MCB1 Flashcards

1
Q

Name 3 cellular organelles present only in eukaryotic cells.

A

Nucleus, mitochondrion, centriole, lysosome, endoplasmic reticulum.

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2
Q

What is the method of introducing foreign DNA into a bacterium?

A

Transformation.

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3
Q

What is the name of the gene transfer into prokaryotic and eukaryotic cells?

A

Into prokaryotic cells: transformation, into eukaryotic cells: transfection.

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4
Q

What is the mechanism of action of penicillin?

A

Inhibits the formation of bacterial cell wall.

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5
Q

Name the chromosome-containing part of a bacterium.

A

Nucleoid region.

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6
Q

Name three characteristics of bacterial DNA that distinguish it from eukaryotic DNA.

A

Shorter, circular, naked, mostly consists of coding region.

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7
Q

What does it mean that viruses are obligate intracellular parasites?

A

They multiply inside the infected cells only.

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8
Q

What infections can be caused by bacteriophages (2)?

A

Lytic and lysogenic infection

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9
Q

What is the name of the hypothesis describing the origin of eukaryotic cells?

A

Endosymbiotic hypothesis.

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10
Q

What parameters influence the resolution power of a light microscope?

A

Wavelength of light, refractive index, aperture angle of objective lens.

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11
Q

How can you define the limit of resolution?

A

The shortest distance whose two endpoints can be distinguished from one another.

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12
Q

Name the magnifying components of the light microscope.

A

Objective lens, ocular lens.

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13
Q

How can you calculate the magnification of the light microscope?

A

Magnification of objective lens × magnification of ocular lens (eyepiece).

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14
Q

Describe the image that can be seen in the light microscope.

A

magnified in two steps, inverse, virtual

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15
Q

Name two fixatives used in microscopy.

A

formaldehyde, glutaraldehyde, osmiumtetroxide, etc.

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16
Q

Which technique is suitable to visualize a specific protein in the cell?

A

immunocytochemistry

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17
Q

Name two electron microscopic methods which give three dimensional image of the specimen.

A

angular shadowing, freeze-etching technique, freeze-fracture technique, scanning electron microscopy

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18
Q

Name two electron microscopic methods which are suitable to study isolated organelles.

A

angular shadowing, rotary shadowing, negative staining, etc.

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19
Q

Which techniques use the deposition of metals on surfaces in electron microscopy? Give two examples.

A

angular shadowing, rotary shadowing, scanning electron microscopy, replica-technique

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20
Q

Which are the subcellular fractions and in which order are they generated by differential centrifugation?

A

nuclear fraction mitochondrial fraction → microsomal fraction → ribosomal fraction > cytosol

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21
Q

Which cellular organelles can be found in the microsomal fraction?

A

Golgi complex, RER (rough endoplasmic reticulum), SER (smooth endoplasmic reticulum)

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22
Q

Which separation methods are used during 2D electrophoresis of proteins?

A

isoelectric focusing and SDS polyacrylamide gel electrophoresis

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23
Q

What charge do proteins have at the end of isoelectric focusing?

A

no net charge

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24
Q

What charge do proteins have at the end of SDS polyacrylamide gel electrophoresis?

A

negative

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25
Q

Which electrophoretic method is suitable for the separation of proteins according to their molecular mass?

A

SDS polyacrylamide gel electrophoresis

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26
Q

Towards which electrode do nucleic acids move during electrophoresis?

A

towards the positive electrode

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27
Q

Name 2 separation methods which fractionate particles mostly according to their molecular mass.

A

gel filtration, SDS polyacrylamide gel electrophoresis, hypopycnic density gradient centrifugation

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28
Q

Name 2 separation methods where fractionation is independent of the molecular mass of the particles.

A

ion-exchange chromatography, isoelectric focusing, affinity chromatography, isopycnic density gradient centrifugation

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29
Q

During gel filtration, the elution volume of substance ‘A’ is larger than that of substance ‘B’. What conclusion can be drawn from this?

A

the molecular mass of substance ‘B’ is larger than the molecular mass of substance ‘A’

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30
Q

What kind of ligands can be used during affinity chromatography to separate what kind of substances? Give 2 examples.

A

antigene-antibody, enzyme-substrate, hormone-receptor, oligo(dT)-poly(A)+ mRNA, etc.

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31
Q

Which separation method is suitable for the separation of poly(A)+ mRNAs from total cellular RNA?

A

oligo(dT) cellulose affinity chromatography

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32
Q

What type of bonds stabilize the DNA double helix?

A

H-bonds

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33
Q

What are the basic rules of H-bond formation between bases in nucleic acids?

A

purines with pyrimidines; A with T (in DNA) or with U (in RNA); G with C (in DNA as well as in RNA)

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34
Q

What are the two main principles of the interaction between the two strands of nucleic acids?

A

complementarity, antiparallelity

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35
Q

What is the definition of denaturation of nucleic acids?

A

The disruption of H-bonds

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36
Q

What is a nucleoside composed of?

A

base + pentose

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37
Q

What is a nucleotide composed of?

A

base + pentose + phosphate group

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38
Q

Which pentose is found in DNA?

A

deoxyribose

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39
Q

Which pentose is found in RNA?

A

ribose

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40
Q

What is the difference between ribose and deoxyribose?

A

deoxyribose lacks the OH-group at the 2’ C-atom

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41
Q

What bond links the neighbouring nucleotides together in a nucleic acid strand?

A

phosphodiester bond

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42
Q

What is antiparallelity?

A

the direction of phosphodiester bonds is opposite in the complementary strands of double-stranded nucleic acids

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43
Q

What is the melting point of DNA?

A

the temperature required to denature 50% of the DNA sample

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44
Q

What is hyperchromicity?

A

the increase of UV light absorption during denaturation of DNA

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45
Q

What are purine and pyrimidine bases?

A

purines: A, G; pyrimidines: C, T, U

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46
Q

In which nucleic acids are the different bases found?

A

DNA: A, G, C, T; RNA: A, G, C, U

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47
Q

Name a chemical that can precipitate DNA!

A

ethanol, trichloroacetic acid, etc.

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48
Q

What is the charge of nucleic acids at neutral pH?

A

negative

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49
Q

What is the reason for the negative charge of nucleic acids?

A

due to the phosphate groups

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50
Q

Name two chemicals that can cause DNA denaturation!

A

alkaline solutions, formamide, urea, etc.

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51
Q

Name a chemical that can cause the denaturation of RNA!

A

formaldehyde

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52
Q

What explains the differences between the melting points of DNA of different species?

A

the difference between the A+T/G+C ratios in the different DNA molecules

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53
Q

What is a ribozyme?

A

RNA possessing catalytic activity

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54
Q

Name an acidic amino acid!

A

aspartic acid, glutamic acid

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55
Q

Name a basic amino acid!

A

lysine, arginine, histidine

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56
Q

What is the general structure of an amino acid like?

A

a central C atom attached to four groups: a H atom, a carboxyl group, an amino group and a side chain

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57
Q

What is the primary structure of proteins?

A

the order of amino acids

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58
Q

Name the bond that links the amino acids together in the primary structure of proteins!

A

peptide bond

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59
Q

What are the two major forms of the secondary structure of proteins?

A

a helix, B sheet

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60
Q

What is the name of a functional unit in the tertiary structure of proteins?

A

domain

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61
Q

What kind of proteins are involved in the folding of proteins in vivo?

A

chaperones

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62
Q

What makes an amino acid acidic?

A

carboxyl group in the side chain

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63
Q

Name two proteins possessing quaternary structure!

A

haemoglobin, insulin

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64
Q

How do enzymes change the activation energy of the catalyzed reactions?

A

decrease it

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65
Q

Give a definition of the term ‘proteome’!

A

all the proteins present in a cell

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66
Q

Name two carotenoids!

A

B-carotene, retinal

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67
Q

Name three steroid compounds!

A

cholesterol, testosterone, vitamin D

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68
Q

Which steroid is a membrane-component?

A

cholesterol

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69
Q

Name three hexose sugars!

A

glucose, galactose, fructose

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70
Q

Name two glucose-polysaccharides!

A

glycogen, starch

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71
Q

Name two glycosaminoglycans!

A

chondroitin sulphate, hyaluronic acid

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72
Q

What is the name of the recognition sequence of restriction endonucleases?

A

palindromic sequence

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73
Q

Give an example for a palindromic sequence containing six base pairs.

A

GAATTC

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74
Q

Name two types of enzymes that are capable of recognizing palindromic sequences!

A

restriction endonucleases, modification methylases

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75
Q

What kind of DNA ends can be generated by restriction endonucleases?

A

blunt ends, cohesive (sticky) ends

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76
Q

Name two methods in which restriction endonucleases have a paramount role!

A

cloning, genomic library

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77
Q

Name two vectors used in molecular biology!

A

plasmid, adenovirus

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78
Q

What is the name of the vector the DNA-insert of which can be transcribed in a host cell?

A

expression vector

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79
Q

Name three sequences that can be isolated only from the genomic library and not from the cDNA library!

A

promoter, satellite DNA, intron

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80
Q

Would you name the three steps of a PCR cycle in the correct order?

A

denaturation, primer binding, DNA synthesis

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81
Q

Name two methods used for amplification of a DNA fragment!

A

PCR, cloning

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82
Q

Name the type of polymerase chain reaction that can be used to quantitate a specific nucleic acid sequence during the reaction!

A

real-time PCR

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83
Q

What is molecular hybridisation?

A

Renaturation of a denatured nucleic acid with a labelled probe

Molecular hybridisation is commonly used in various techniques such as in situ hybridisation and northern blotting.

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84
Q

Name two enzymes required to prepare a cDNA library!

A

Reverse transcriptase, DNA ligase, restriction endonuclease

These enzymes are essential for synthesizing complementary DNA (cDNA) from mRNA.

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85
Q

Which one is tissue specific: a cDNA library or a genomic library?

A

cDNA library

A cDNA library is derived from mRNA transcripts, reflecting gene expression in specific tissues.

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86
Q

Give an example for the physical, the chemical, and the biological gene transfer!

A

Physical: microinjection, electroporation, gene gun; Chemical: transfection, liposome; Biological: virus vector

These methods are used to introduce genetic material into cells.

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87
Q

What is the name of animals whose genome contains an artificially introduced gene, and this gene is inherited to the offspring?

A

Transgenic animals

Transgenic animals are created for various purposes, including research and agriculture.

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88
Q

What does the abbreviation GMO stand for?

A

Genetically modified organism

GMOs are organisms whose genetic material has been altered using genetic engineering techniques.

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89
Q

Which methods can be used to generate genetically modified organisms (2)?

A

Microinjection of transgenes into a zygote, manipulation of embryonic stem cells

These methods allow for the introduction of new genetic material into organisms.

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90
Q

What domains do zinc finger nucleases contain (2)?

A

DNA-binding domain and endonuclease domain

Zinc finger nucleases are designed for targeted genome editing.

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91
Q

What are the two most important molecular components of the CRISPR/Cas9 system?

A

CRISPR RNA molecule (targeting RNA or guide RNA) and the Cas9 protein

These components work together to enable precise editing of the genome.

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92
Q

What is the function of the targeting RNA (gRNA) in the CRISPR/Cas9 system?

A

gRNA binds to the specific DNA sequence in the genome by complementary base pairing

This specificity is crucial for the accuracy of genome editing.

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93
Q

What is the role of the Cas9 protein in the CRISPR/Cas9 system?

A

Cas9 protein is an endonuclease that cleaves both DNA strands of the targeted region

This cleavage is necessary for introducing genetic modifications.

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94
Q

What genetic changes can be induced in a specific region of the genome by targeted gene manipulation techniques (2)?

A

Gene inactivation (knock out mutation) or gene correction (knock in mutation)

These techniques are used to study gene function and treat genetic diseases.

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95
Q

What is an antisense oligonucleotide?

A

An oligonucleotide that can inhibit mRNA function by complementary base-pairing

Antisense oligonucleotides are used in therapeutic applications to modulate gene expression.

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96
Q

What is the name of the RNA molecules responsible for RNA interference?

A

siRNAs

Small interfering RNAs (siRNAs) play a key role in regulating gene expression through RNA interference.

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97
Q

What is the physiological function of siRNAs?

A

Regulation of gene expression

siRNAs help to silence specific genes, playing a crucial role in cellular processes.

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98
Q

Name a method suitable for specific inhibition of protein function!

A

Intracellular antibodies, expression of dominant inhibitory proteins, peptidomimetics, competitive inhibitors

These methods can be used to study protein function or develop therapeutic strategies.

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99
Q

Name two methods for the identification of proteins by using specific antibodies!

A

Immunocytochemistry, immunoprecipitation, Western blotting

These techniques are essential for studying protein expression and interactions.

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100
Q

What is the role of mRNA and oligo(dT) added to an in vitro cDNA synthesizing system?

A

mRNA: template, oligo(dT): primer

This combination is crucial for synthesizing cDNA from mRNA.

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101
Q

Name two methods capable of proving that the actin gene is expressed in liver cells!

A

Western blotting, immunocytochemistry, reverse transcription PCR

These methods can confirm gene expression at the protein or mRNA level.

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102
Q

What is the difference between dTTP and ddTTP?

A

The absence of an -OH group at the 3’-position in ddTTP

This structural difference is critical in DNA synthesis and sequencing.

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103
Q

Write an example of a technique where the nucleic acid probe sequence used is not labeled

A

sequencing chip, SNP-chip, cDNA-chip

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104
Q

Name the main steps of Illumina sequencing in order

A

library construction, amplification, sequencing, data analysis

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105
Q

What are the specific properties of the single nucleotide building blocks used in the sequencing step of the Illumina method?

A

a cleavable blocking molecule is attached to the 3’ OH group of the nucleotide and a fluorescent dye molecule, also cleavable, is attached to its base

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106
Q

What kind of a signal is detected by the machine after incorporation of a nucleotide during Illumina sequencing?

A

fluorescence

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107
Q

Which scientific term describes the property of simultaneously sequencing a very large number of DNA fragments in case of Illumina and Proton sequencing?

A

massively parallel

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108
Q

What kind of nucleotides are used in Proton sequencing?

A

unlabeled, unmodified/normal dNTPs

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109
Q

What change is detected after incorporation of a nucleotide during Proton sequencing?

A

pH decrease

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110
Q

What kind of nucleic acids can be sequenced using the Nanopore method?

A

single-stranded DNA or RNA

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111
Q

What kind of signal is detected by the machine during Nanopore sequencing during the incorporation of a nucleotide?

A

change in current

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112
Q

What are cDNA-chips used for?

A

to analyze the expression of many (all) genes in a cell

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113
Q

How could you make visible the result of molecular hybridization?

A

e.g. by autoradiography, fluorescence microscopy

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114
Q

What is the purpose of fluorescence in situ hybridization (FISH)?

A

localization of a specific nucleic acid sequence by hybridization of a fluorescently labeled probe

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115
Q

What are the types of fluorescence in situ hybridization (FISH) based on the position of the cell along its cell cycle?

A

interphase FISH and metaphase FISH

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116
Q

What kind of information about the DNA sequence of interest can be obtained from the results of fluorescence in situ hybridization (FISH)?

A

presence, localization, amount

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117
Q

How many fluorescent signals can be seen in the results of fluorescence in situ hybridization (FISH) in a single healthy diploid cell, when using a probe specific for a given autosomal chromosomal region?

A

two

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118
Q

Give three examples of the application of fluorescence in situ hybridization (FISH)

A

analysis of localization of specific genes, analysis of specific chromosomal regions (e.g. telomere, centromere), detection of genetic abnormalities (e.g. deletion, gene amplification, chromosomal translocation), detection of all chromosomes in a cell

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119
Q

Name the main components of the nucleus

A

nuclear envelope, nucleoplasma, chromatin, nucleolus, nuclear matrix

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120
Q

Which proteins connect chromatin to the inner surface of the nuclear membrane?

A

lamin proteins

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121
Q

How could you classify heterochromatin on the basis of its location?

A

marginal/peripheral, nucleolus-associated, diffuse heterochromatin

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122
Q

What is the functional difference between eu- and heterochromatin?

A

heterochromatin is inactive, euchromatin contains transcriptionally active parts

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123
Q

Name the components of the nucleolus (4)

A

fibrillar center, fibrillar component, granular component, nucleolus-associated heterochromatin

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124
Q

What is the transport protein and G-protein involved in transport through the nuclear pores?

A

transport protein: importin, exportin; G-protein: Ran

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125
Q

What is the enzyme activity of Ran?

A

GTPase

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126
Q

Name the two types of karyopherins

A

importins, exportins

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127
Q

In what form can DNA be found in interphase cells and in dividing cells?

A

interphase cells: chromatin, dividing cells: chromosome

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128
Q

Name the chemical components of chromatin (4)

A

DNA, proteins (histones and non-histones), ions, RNA

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129
Q

Name 2 chemical modifications that are characteristic of histones

A

phosphorylation, acetylation

130
Q

What is the difference between constitutive and facultative heterochromatin?

A

constitutive: permanently inactive form, facultative: in certain circumstances may be activated

131
Q

What is a nucleosome made of?

A

histone octamer and DNA

132
Q

Name the morphological levels of chromatin organisation in the correct order

A

beads-on-a-string, solenoid, looped domains, metaphase chromosome

133
Q

Name 2 nonhistone proteins with regulatory function

A

TATA factor, AP-1, SRE, CREB

134
Q

Name 2 nonhistone proteins with enzymatic function

A

RNA polymerases, DNA polymerases, nucleases, ligases

135
Q

What kind of RNA molecules can be found in chromatin? Name 2 of them

A

pre-mRNA, pre-rRNA, snRNA, snoRNA

136
Q

Name a region of chromatids where microtubules bind during cell division

A

kinetochore, telomeric region

137
Q

Name the region of chromosomes where sister chromatids are attached to each other

A

centromere

138
Q

Give 2 examples of tandemly repeated genes

A

rRNA genes, tRNA genes, histone genes

139
Q

Which are the repetitive sequences that can be used as highly polymorphic genetic markers? (2)

A

minisatellites, microsatellites

140
Q

Where are the highly repetitive sequences located in the chromosomes? (2)

A

in the centromeric and telomeric regions

141
Q

Name a polyglutamine disease

A

Huntington’s disease

142
Q

What type of mutation is characteristic of Huntington’s disease?

A

trinucleotide repeat expansion

143
Q

What does the abbreviation VNTR stand for?

A

variable number of tandem repeats

144
Q

Give 2 examples of proteins coded by gene families

A

globin, cytoskeleton, cell membrane receptors, protein kinases, transcription factors

145
Q

What does pseudogene mean?

A

members of gene families, which became inactive by mutations

146
Q

What does it mean, that a gene is amplified in the genome?

A

the increase in the copy number of a gene in the genome

147
Q

Give an example of a gene amplified in the genome!

A

rRNA genes, c-myc in certain tumors, etc.

148
Q

Which human chromosome contains Alu sequences?

A

all of them

149
Q

Give an example for a retrotransposon!

A

viral retrotransposons, Alu sequences, etc.

150
Q

What are the two main phases of the cell cycle?

A

interphase and cell division

151
Q

What are the 3 main phases of the interphase?

A

G1, S, G2 phases

152
Q

What is the amount of DNA in a G1 phase cell?

A

2n, diploid

153
Q

What is the amount of DNA in a G2 phase cell?

A

4n, tetraploid

154
Q

Name a cell type which resides in the G0 phase!

155
Q

Name two processes occurring during the S phase!

A

replication, synthesis of histones, translocation of DNA polymerase into the nucleus, etc.

156
Q

What is the name of the procedure when all cultured cells are brought into the same phase of the cell cycle?

A

synchronisation

157
Q

Name two methods which are suitable for the synchronisation of a cell population!

A

serum starvation, mitotic shake-off, treatment with colchicine, etc.

158
Q

Which method can be used to separate cells on the basis of their DNA content?

A

flow cytometry (FACS)

159
Q

Would you name 2 mitogenic substances?

A

phytohaemagglutinin, PDGF, EGF, FGF, etc.

160
Q

What are the components of MPF?

A

cyclin and cyclin dependent kinase

161
Q

What kind of catalytic activity do the Cdk enzymes possess?

A

serine/threonine specific protein kinase activity

162
Q

What are the major phases of mitosis?

A

prophase, metaphase, anaphase, telophase, cytokinesis

163
Q

Name a protein phosphorylated by MPF!

A

histone H1, lamin, microtubule associated proteins, etc.

164
Q

Name the four main components of the mitotic spindle!

A

kinetochore, polar, chromosomal and astral microtubules

165
Q

Which type of microtubules is responsible for the separation and movement of chromatids?

A

kinetochore microtubules

166
Q

Which type of microtubules is responsible for the elongation of the cell as well as for the moving off of the two poles?

A

polar microtubules

167
Q

Name the protein complexes that hold sister chromatids together!

A

cohesin complexes

168
Q

Name the enzyme that cleaves cohesin complexes between sister chromatids!

169
Q

In which phase of mitosis are the chromatids separated from each other?

170
Q

Which element of the cytoskeleton is responsible for cytokinesis?

A

actin filaments

171
Q

What kind of cell division has a role in germ cell formation?

172
Q

What is the DNA content of those cells which are produced by meiosis?

A

n, haploid

173
Q

What happens in the anaphase of the 1 meiotic cell division?

A

homologous chromosomes separate from each other

174
Q

What happens in the anaphase of the 2nd meiotic cell division?

A

sister chromatids separate from each other

175
Q

What is crossing over?

A

exchange of genetic material between homologous chromosomes during meiosis

176
Q

What is the meaning of the semiconservative nature of replication?

A

one chain of the replicated DNA is the original and the other is the newly synthesized one

177
Q

What is the function of template during replication?

A

helps nucleotide incorporation by complementary base-pairing

178
Q

Why is DNA replication primer-dependent?

A

because DNA polymerases are unable to initiate DNA synthesis

179
Q

What is the name of the continuously replicated strand of the replication fork?

A

leading strand

180
Q

What is the name of the short DNA segments that are synthesized from the lagging template strand of the replication fork?

A

Okazaki-fragments

181
Q

What is the name of the site where DNA replication begins?

A

origo (origin of replication)

182
Q

Which enzyme causes relaxation of DNA during replication?

A

topoisomerase I

183
Q

Which enzyme cleaves the hydrogen bonds at the replication fork?

184
Q

What is the function of primase?

A

it is responsible for the synthesis of RNA primers

185
Q

What is proofreading?

A

the removal of non-complementary nucleotides incorporated during DNA replication

186
Q

What kind of enzyme activities does DNA polymerase III have?

A

5’→3 elongation, 3’→5 exonuclease

187
Q

What kind of enzyme activities does DNA polymerase I have?

A

5’→3 elongation, 5’→3’ exonuclease, 3’ →5’ exonuclease

188
Q

What is the function of the 3’ 5’ exonuclease activity during replication?

A

proofreading

189
Q

What is the function of the 5’ →3 exonuclease activity during replication?

A

primer degradation

190
Q

What is the name of the enzyme that joins the Okazaki fragments?

A

DNA ligase

191
Q

What kind of enzyme activity does topoisomerase II have?

A

reversible double-stranded endonuclease

192
Q

Which enzyme inhibits shortening of eukaryotic chromosomes?

A

telomerase

193
Q

What is the enzyme activity of telomerase?

A

reverse transcriptase

194
Q

What is the role of telomerase RNA?

A

template for the synthesis of telomere repeats

195
Q

What is the consequence of decreasing proofreading-activity during replication?

A

increasing rate of mutations

196
Q

What kind of DNA damage can be caused by UV irradiation?

A

pyrimidine dimers

197
Q

Which repair system is responsible for the replacement of damaged bases?

A

base excision repair

198
Q

Which enzyme can recognize and remove a damaged base in base excision repair?

A

DNA glycosylase

199
Q

What is the name of the mechanism that removes pyrimidine dimers?

A

nucleotide excision repair

200
Q

What kind of enzyme activity does the excinuclease have?

A

endonuclease

201
Q

Name a human disease with defective nucleotide excision DNA repair!

A

xeroderma pigmentosum

202
Q

Which repair mechanism is responsible for the correction of non-complementary basepairing?

A

mismatch repair

203
Q

Name a human disease with defective mismatch repair!

A

HNPCC (hereditary non-polyposis colon carcinoma)

204
Q

What are the 3 main steps of transcription?

A

initiation, elongation, termination

205
Q

What is the name of the DNA region involved in the initiation of transcription?

206
Q

What are the initial and the final sequences of a transcription unit?

A

initial: promoter, final: terminator

207
Q

What is the name of the transcriptional step that leads to the formation of phosphodiester bonds?

A

elongation

208
Q

What is the direction of RNA synthesis from the point of view of RNA?

209
Q

Name the RNA produced by transcription, but has not been processed yet!

A

primary transcript

210
Q

What are the two components of the RNA polymerase in bacteria during initiation?

A

core enzyme and sigma factor

211
Q

What is the role of the bacterial rho factor?

A

termination of transcription

212
Q

What is the role of the bacterial sigma factor?

A

the initiation of transcription

213
Q

Name the process by which a primary transcript is converted to a mature RNA!

A

RNA processing

214
Q

Which enzyme produces the pre-rRNA in eukaryotic cells?

A

RNA polymerase I

215
Q

What kind of rRNAs are produced from the mammalian pre-rRNA?

A

18S, 28S, 5.8S rRNA

216
Q

Which rRNA is produced outside the nucleolus?

217
Q

What is the name of the DNA region between the 18S and 5.8S rRNA genes?

A

transcribed spacer

218
Q

What kind of process do Christmas-trees show?

A

synthesis of eukaryotic rRNA

219
Q

What is the role of snoRNAS?

A

pre-rRNA processing in eukaryotes

220
Q

At which site is the maturation of ribosomal subunits finished?

221
Q

What is the site of the formation of ribosomal proteins?

A

free ribosomes of the cytoplasm

222
Q

When do ribosomal subunits attach to each other?

A

during initiation of translation

223
Q

What is the name of the pre-mRNA sequences that are absent from the mature mRNA molecules?

224
Q

What is the name of the pre-mRNA sequences that are present even in the mature mRNA?

225
Q

What is the name of the process that removes the introns from the pre-mRNA?

226
Q

What are the components of the spliceosome?

A

pre-mRNA, snRNAs and proteins

227
Q

What are the maturation processes of a pre-mRNA?

A

formation of the cap structure, polyadenylation, splicing

228
Q

Which enzyme produces the pre-mRNAs in eukaryotic cells?

A

RNA polymerase II

229
Q

What is the role of the mediator complex?

A

to connect signaling pathways to the transcriptosome

230
Q

Nucleotides can be changed, added or deleted during mRNA processing. What is the name of this process?

A

RNA editing

231
Q

What is the role of mRNA and tRNA during translation?

A

mRNA: template, tRNA: adapter

232
Q

What kind of molecules take part in amino acid activation?

A

amino acid, ATP, aminoacyl-tRNA synthase

233
Q

What are the products of amino acid activation?

A

aminoacyl-AMP, pyrophosphate

234
Q

Name the molecules that are able to bind to the 3 main loops and to the 3’ end of tRNA.

A

ribosome, mRNA, aminoacyl-tRNA synthase, amino acid

235
Q

What is a monocistronic mRNA?

A

it contains only one open reading frame

236
Q

What is the central dogma of molecular biology?

A

direction of flow of information: DNA → RNA → proteins

237
Q

What is a polycistronic mRNA?

A

It contains more than one open reading frame.

238
Q

What is the start site and the end of an open reading frame?

A

Start: initiation codon, End: stop codon.

239
Q

Which feature of the genetic code means that one amino acid could be coded by more than one codon?

A

Redundancy (degeneration).

240
Q

Which nucleotide of a codon is involved in ‘wobble’?

A

The third nucleotide.

241
Q

Name the enzyme that catalyzes peptide bond formation.

A

Peptidyl transferase.

242
Q

Where can peptidyl transferase be found?

A

It is a ribozyme in the large subunit of the ribosome.

243
Q

The anticodon of a tRNA molecule is 5’-CAU-3’, what is the sequence of the corresponding codon of mRNA (5’—3’)?

A

5’-AUG-3’.

244
Q

Name three antibiotics able to inhibit protein synthesis.

A

Erithromycin, tetracycline, streptomycin, chloramphenicol.

245
Q

What is the polysome made of?

A

A single mRNA molecule and ribosomes.

246
Q

What is the direction of protein synthesis from the point of view of mRNA?

A

5’ → 3’.

247
Q

What is the direction of protein synthesis from the point of view of protein?

A

N terminus - C terminus.

248
Q

What are the 3 repeated steps of the elongation of translation?

A

Binding of aminoacyl-tRNA, peptidyl transferase reaction, translocation.

249
Q

What are the sedimentation constants of the subunits and the whole ribosome in prokaryotes?

A

Subunits: 30S and 50S, Whole ribosome: 70S.

250
Q

What are the sedimentation constants of the subunits and the whole ribosome in eukaryotes?

A

Subunits: 40S and 60S, Whole ribosome: 80S.

251
Q

Which are the energy-dependent processes during translation?

A

Amino acid activation, aminoacyl-tRNA binding, translocation.

252
Q

What does constitutive gene expression mean?

A

A certain gene is continuously expressed at the same rate.

253
Q

What kind of DNA regions build up a bacterial operon?

A

Promoter, operator, structural genes.

254
Q

What kind of an operon is the lactose operon?

A

Inducible operon.

255
Q

What is the effect of the presence of glucose in the medium on the cAMP content of bacteria?

A

Decreases it.

256
Q

What is the effect of the presence of glucose in the medium on the function of lactose operon of bacteria?

A

Decreases it.

257
Q

What protein binds cAMP during the regulation of lactose operon?

A

CAP (catabolite activator protein).

258
Q

What is the name of the DNA region in the lactose operon that binds the repressor?

259
Q

What is the role of lactose in the regulation of lactose operon?

A

Inducer substance.

260
Q

What kind of metabolic processes are regulated by inducible operons?

A

Breakdown processes.

261
Q

What kind of an operon is the bacterial tryptophan operon?

A

Repressible operon.

262
Q

What is the role of tryptophan in the regulation of tryptophan operon?

A

Corepressor.

263
Q

To what does tryptophan bind during the course of regulating the tryptophan operon?

A

To the repressor.

264
Q

How does the presence of tryptophan affect the activity of the tryptophan operon?

A

decreases it

265
Q

What kind of metabolic processes are regulated by repressible operons?

A

biosynthetic processes

266
Q

Name a cis-acting regulatory element!

A

promoter, operator, enhancer

267
Q

What is the most characteristic feature of housekeeping genes?

A

they are active in all types of cells

268
Q

Name two levels at which gene expression can be regulated in eukaryotic cells!

A

transcription, RNA processing, RNA transport

269
Q

Name an epigenetic mechanism of gene regulation!

A

histone acetylation, DNA methylation

270
Q

Name a process involved in the regulation of mRNA processing!

A

alternative splicing, RNA editing

271
Q

Give the definition of the term ‘constitutive splicing’!

A

the process producing a single kind of mRNA from a pre-mRNA

272
Q

What are the two main mechanisms of protein breakdown in eukaryotic cells?

A

lysosomal digestion, ubiquitin-proteasome degradation

273
Q

What is the fate of polyubiquitinated proteins in the cell?

A

become degraded by proteasomes

274
Q

What domains of a transcription factor are absolutely necessary for its function?

A

DNA binding domain, activator domain

275
Q

Name two groups of eukaryotic transcription factors!

A

helix-turn-helix, Zn-finger, amphipathic helix

276
Q

Name a Zn-finger protein!

A

TFIIA, steroid receptors, WT-1

277
Q

What is the cause of testicular feminisation?

A

the lack of androgen receptors

278
Q

Where are glucocorticoid receptors located in a target cell not treated with glucocorticoid?

A

in the cytosol

279
Q

Name two disorders that can be caused by malfunction of transcription factors!

A

cancer, endocrine diseases, developmental diseases

280
Q

Name the surfaces of the endoplasmic reticulum!

A

cytoplasmic surface, exoplasmic surface

281
Q

What kind of molecules are synthesized on the rough and on the smooth endoplasmic reticulum?

A

rough endoplasmic reticulum: proteins, smooth endoplasmic reticulum: lipids

282
Q

What kind of proteins are synthesized on the surface of the rough endoplasmic reticulum?

A

secretory proteins, membrane proteins, lysosomal enzymes, proteins of the endoplasmic reticulum and the Golgi complex

283
Q

On which type of ribosomes does protein synthesis start?

A

All proteins synthesis starts on free ribosomes

284
Q

What determines whether a certain protein is synthesized on the rough endoplasmic reticulum?

A

the signal sequence

285
Q

What is the mechanism by which the newly synthesized protein is transported into the lumen of the rough endoplasmic reticulum?

A

cotranslational transport

286
Q

What does protein glycosylation mean?

A

addition of carbohydrates to a protein chain

287
Q

Name a disease associated with the abnormal function of the chaperones present in the rough endoplasmic reticulum!

A

cystic fibrosis, familial hypercholesterolaemia

288
Q

Name the two types of secretion!

A

constitutive and regulated secretion

289
Q

Name two examples of constitutive secretion!

A

secretion of matrix proteins, antibodies, albumin; replacement of cell membrane components

290
Q

Name two amino acids that are capable of binding to carbohydrate side chains in a protein!

A

asparagine, serine, threonine, hydroxylysine

291
Q

Name two carbohydrates which are components of glycoproteins!

A

glucose, mannose, N-acetyl-glucosamine

292
Q

Name the types of endocytosis (3)!

A

phagocytosis, pinocytosis, receptor-mediated endocytosis

293
Q

In which form is cholesterol transported in the blood?

A

LDL particles

294
Q

What kind of mechanism is used by the cells to take up LDL particles?

A

receptor-mediated endocytosis

295
Q

What disease is caused by the absence of LDL receptors?

A

familial hypercholesterolaemia

296
Q

Name three proteins involved in vesicular transport!

A

ARF, adaptin, targeting proteins, Rab proteins, chaperone proteins

297
Q

Name two of the most frequently produced free radicals in the cells!

A

superoxide free radical, hydroxyl free radical

298
Q

Which enzyme produces the superoxide free radical during phagocytosis?

A

NADPH oxidase

299
Q

What kind of compounds are produced by the reduction of an oxygen molecule by 1, 2, 3, or 4 electrons?

A

superoxide free radical, hydrogen peroxide, hydroxyl free radical, water

300
Q

What kind of enzymes are responsible for the inactivation of the superoxide free radical and hydrogen peroxide, respectively?

A

superoxide: superoxide dismutase, hydrogen peroxide: catalase, peroxidase

301
Q

Free radicals degrade the unsaturated fatty acid components of the membranes. What is the name of this process?

A

lipid peroxidation

302
Q

Name two lysosomal storage diseases!

A

Tay-Sachs disease, I-cell disease, Gaucher disease, Niemann-Pick disease

303
Q

What kind of enzymes are present in lysosomes?

A

acid hydrolases

304
Q

The lysosomes can digest cellular organelles. What is the name of this process?

A

autolysis (autophagy)

305
Q

What is the signal that targets lysosomal enzymes to lysosomes?

A

mannose-6-phosphate

306
Q

Name the three main functions of the smooth endoplasmic reticulum!

A

biotransformation, lipid synthesis, storage of calcium

307
Q

What is the effect of phenobarbital on the cytochrome P450 system of liver cells?

A

induces it

308
Q

List the steps of biological oxidation and their sites in the cell

A

Glycolysis: cytoplasm, Citric acid cycle: mitochondrial matrix, Terminal oxidation: inner membrane of mitochondrion

Biological oxidation involves the conversion of glucose to ATP through glycolysis, the citric acid cycle, and terminal oxidation.

309
Q

What are the four main structural elements of a mitochondrion?

A
  • Outer membrane
  • Intermembrane space
  • Inner membrane
  • Mitochondrial matrix

These components play crucial roles in mitochondrial function, including energy production.

310
Q

What is the cause of the different permeability of the inner and outer mitochondrial membranes?

A

Inner membrane: impermeable due to cardiolipin, Outer membrane: permeable due to porin

Cardiolipin is a unique phospholipid found in the inner membrane, while porins are proteins that form channels in the outer membrane.

311
Q

Name the three main types of proteins of the inner mitochondrial membrane.

A
  • Transport proteins
  • Proteins of the electron transport chain
  • ATP synthase

These proteins are essential for mitochondrial function and energy production.

312
Q

How is pyruvate taken up by mitochondria?

A

By H+/pyruvate symporter

This symporter allows the transport of pyruvate into the mitochondria coupled with protons.

313
Q

What is the motive force of the mitochondrial ATP synthase?

A

The electrochemical proton gradient

This gradient is created by the electron transport chain and drives ATP synthesis.

314
Q

What are the subunits of the mitochondrial ATP synthase?

A
  • Fo
  • Fi

These subunits work together to synthesize ATP from ADP and inorganic phosphate.

315
Q

Where is the site of synthesis of the proteins and RNAs of mitochondrial ribosomes?

A
  • Proteins: on free ribosomes of the cytoplasm
  • rRNAs: in the mitochondrial matrix

This separation of synthesis locations reflects the dual genetic origins of mitochondria.

316
Q

How can proteins enter the mitochondrion?

A

By posttranslational transport

This process involves the transport of fully synthesized proteins into the mitochondria.

317
Q

What is the function of chaperones in the transport of proteins into mitochondria?

A

They unfold the protein chain

Chaperones assist in the proper import and folding of proteins within mitochondria.

318
Q

Where is the pH-value higher: in the mitochondrial matrix or in the intermembrane space?

A

In the mitochondrial matrix

The higher pH in the matrix is important for various mitochondrial functions, including ATP synthesis.

319
Q

What is the function of the Fo component of the mitochondrial ATP synthase?

A

Proton channel

The Fo component facilitates the movement of protons across the inner mitochondrial membrane.

320
Q

Name three disorders caused by mitochondrial DNA damage.

A
  • Mental dementia
  • Cardiomyopathy
  • Optic nerve atrophy
  • Glomerulopathy

Mitochondrial DNA damage can lead to a variety of diseases due to impaired energy production.

321
Q

What is the name of the phenomenon where a cell contains both normal and mutated mitochondrial DNA molecules?

A

Heteroplasmy

Heteroplasmy can affect the severity and expression of mitochondrial diseases.