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Molecular Medicine > Cell Functioning > Flashcards

Cell Functioning Flashcards

1
Q

What does a Ligand-Receptor complex function as in Intracellular Signalling

A

Works as a transcription factor

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2
Q

What causes the cell to proceed from the G2 phase into the M phase?

A

Phosphorylated Mitotic Substrates

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3
Q

What type of adaptor is used the in MAPK pathway

A

SH2 adaptor

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4
Q

Which amino acids have OH groups? What is the significance of this?

A

Serine, Tyrosine, Threonine This enable the amino acid to be phosphorylated

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5
Q

What is the main mechanism used in Hydrophilic signalling

A

Protein kinases are activated resulting in: -Proteins with altered functions -Transcription factors activated

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6
Q

What is PP2B also called? What does it do?

A

A phosphoserine and Phosphotheronine Phosphatase It is also called Calcineurin (binds Ca to get activated)

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7
Q

What enables two BAX proteins to bind to each other? How does it do this?

A

BAD binds to BCL2, preventing it from binding to BAX, enabling BAX to bind to another

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8
Q

What does the structure of PKA consist of

A

It is tetrameric: -2 regulatory subunits -2 catalytic subunits

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9
Q

What is the role of Heparon Sulphate Proteoglycans

A

Bind growth factors such as FGF and PDGF restricting their action

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10
Q

What are the variable properties that are manipulated in beads that are used in protein purification

A

Affinity for proteins (some won’t stick to beads)

Size-exclusion (some proteins will get trapped)

Ion-exchange (proteins with opposite charge will stick)

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11
Q

What are autoimmune diseases caused by?

A

Not enough apoptosis of antibody producing B-cells after infection

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12
Q

What two types of stem cells are there

A

embryonic stem cells adult stem cells

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13
Q

What are selectins

A

Transmembrane proteins that bind carbohydrates on another cell’s surface

Used for cellular adhesion

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14
Q

What is FGF and what role does it play

A

Growth Factor

Fibroblast

Growth Factor.

Crucial role in control of development

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15
Q

How many amino acids does a kinase consist of

A

250 - 300 amino acids

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16
Q

What two ligands are predominantly involved in both the PI3K and MAPK pathways

A

EGF (Epidermal Growth Factor)

PDGF (Platelet Derived Growth Factor).

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17
Q

What is the role of Tetracylins

A

Blocks the A site of 30S ribosomal subunit of prokaryotes

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18
Q

What are the products that exit the Golgi after protein processing

A

Secretory Vesicle

Membrane Vesicle

Lysosomal Vesicle

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19
Q

What causes the hairpin loops from pri-miRNA to be cleaved off into separate ones? What does this form?

A

Drosha and DCGR8 Pre-miRNA

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20
Q

What is the enzyme that aids peptide bond formation in Translation?

A

Peptidyl Transferase

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21
Q

How does a Tyrosine Kinase Receptor get activated?

A

Dimerisation of catalytic sites

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22
Q

What amino acid does CDK phosphorylate?

A

Serine and Threonine

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23
Q

What three things does the Wnt pathway play an important role in?

A

Embryogenesis Proliferation of colorectal epithelia Bone formation

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24
Q

Which direction does DNA replication occur

A

5’ —> 3’

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25
Q

What is SDS-PAGE used for

A

To separate and identify proteins

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26
Q

How long is one tRNA

A

75 nucleotides long

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27
Q

What is the adaptor used in the PI3K Pathway

A

SH2 adaptor

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28
Q

How can the E3 ligase subunit be changed to enable it to bind to a protein?

A

Phosphorylation

Ligand binding (causes allosteric transition)

Protein subunit addition (causes allosteric transition)

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29
Q

What is the main cause of the malfunctioning of the proteasome pathway?

A

Intracellular accumulation of misfolded proteins

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30
Q

Describe Inside-out activation of integrins

A

1: Talin is phosphorylated and activated 2: Activated talin binds to integrin and activates it

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31
Q

What shape is the G Protein coupled receptor? How many times does it span the membrane

A

Serpentine in shape Spans the membrane 7 times

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32
Q

What is the role of initiator caspase 8

A

It cleaves procaspases into effector caspases

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33
Q

What molecular interactions enable a tertiary protein structure to be formed

A

H bonds Ionic bonds Hydrophobic interaction VDW forces

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34
Q

What are two things that regulate gene expression

A

Chromatin structure

Signal transduction (environmental signals causing transcription factors to get activated)

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35
Q

What is the DISK made up of?

A

Death ligand

Death receptor

Adaptor Protein

Procaspase 8

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36
Q

What are the three groups that are cleaved off the rRNA strand, once is has been chemically modified

A

18s RNA (contributes to small ribosomal subunit - 40s) Contributes to Large Ribosomal subunit (60s) 5,85s RNA 28s RNA

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37
Q

What are two methods of Transformation in protein recombination

A

Electropolation (creates holes by current)

Chemicals (Ca salts + Heat Shock)

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38
Q

What constitutes the secondary level of protein structure

A

Backbone interaction (H bonds) making a structured chain

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39
Q

Name the three most common Hydrophobic first messengers

A

Steroid hormones

Thyroid hormones

Vitamins

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40
Q

What is a polyribosome

A

A mRNA molecule and two or more ribosomes that make up a complex

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41
Q

What form of energy is used in the elongation stage of Translation? What processes is it used for?

A

GTP is used as energy 1: When the tRNA attaches to the A site 2: When the ribosome is translocated to make space for another tRNA

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42
Q

What does quinobnes do? What are two examples?

A

antibiotic that inhibits topoisomerase Norfloxacin (prokaryotes only) Etoposide

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43
Q

What happens to RISK

A

The passenger strand is removed from complementary guide strand

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44
Q

In PAGE, how would one estimate the mass of a protein

A

For proteins of both known and unknown masses - Plotting Rf (relative migration distance) vs. log of its mass

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45
Q

What is the function of Axin and APC

A

Axin and APC both act as scaffold proteins in the degradation complex formed in the Wnt Pathway

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46
Q

Describe the process of cell migation

A

Makes use of transient adhesion

1: Protrusion of cell at leading edge (direction of movement) using actin filaments
2: Adhesion at leading ends using integrins
3: Deadhesion at trailing edge using inside-out signal to let go

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47
Q

What are Agiopoeitins and what important role do they play?

A

Growth factor Plays an important role in angiogenesis and cell adhesion of haematopoetic stem cells to their stem cell niche

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48
Q

What amino acid does Ca Calmoduin dependent kinase phosphorylate?

A

Serine and Threonine

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49
Q

What are the effector enzymes, 2nd messengers and kinase cascades associated with the Gq pathway?

A

Effector Enzyme - Phospholipase C

2nd messenger - DAG/IP3 Kinase

Cascade - Ca Calmodulin/PKC

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50
Q

What types of cellular junctions use Cadherins

A

Adherens Junction

Desmosomes

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51
Q

What two main regulators of cell proliferation

A

Proto-oncogenes

Growth inhibitors

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52
Q

What is the immediate result of activation of heterotrimeric G proteins

A

Activation of effector enzymes

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53
Q

What cleaves the head of the hairpin off pre-miRNA? What forms as a result?

A

Dicer and TRBP RISC RNA Induced silencing complex

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54
Q

What happens in the elongation stage of transcription

A

– RNA polymerase form elongation (replication ) bubble

– Nucleotides are added

– RNA/DNA hybrids are formed

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55
Q

What is an indirectly labelled probe in FISH called

A

Hapten An antibody can be raised against it which makes it flourescent

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56
Q

What are ICAMs

A

Transient (unstable) cell-cell adhesion molecules that do not interact with the cytoskeleton of either cell

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57
Q

What two types of secondary protein structure are there

A

Alpha helix

Beta sheet

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58
Q

What do Aminoglycoside Antibiotics do

A

Modify ribosomal proteins

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59
Q

What causes a bacterial genome to become compacted? By how much is it compacted?

A

Loop domains Supercoiling within loop domains It is compacted 1000 fold

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60
Q

What binds to the promotor

A

RNA Polymerase

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61
Q

Which steps of the proteosome function require ATP

A

Unfolding protein Feeding protein in

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62
Q

What regulates the process of ribosomal subunits dissociating at the end of translation?

A

Releasing Factors (eRF’s)

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63
Q

What are the effector enzymes, 2nd messengers and kinase cascades associated with the Gs pathway?

A

Effector Enzyme - Adenylate Cyclase

2nd messenger - cAMP

Kinase Cascade - PKA

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64
Q

What are the Purine Bases

A

G and A

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65
Q

What is the function of 2nd messengers

A

To activate kinases

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66
Q

Where do the sidechains of hydrophilic proteins point

A

Point to the centre

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67
Q

What is the function of the N terminal lobe of a kinase

A

Binds ATP

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68
Q

What is the role of Nuclear RNAi

A

Guide strand (of the mRNA/miRNA complex) directs Ago-2 to promotor regions of genes and Ago-2 methylates them, turning off the gene

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69
Q

What two molecules inhibit the elongation step of translation in bacteria

A

Macrolide

Peptidal Transferase Inhibitors

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70
Q

What is PAGE

A

Poly-acrylamide gel electrophoresis

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71
Q

What is one disease that can result from an inhibited Wnt pathway

A

Rheumatoid Arthritis

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72
Q

Describe the general pattern of digestive processes mediated by the lysosome

A

1: Protein taken into cell 2: Enters Early Endosome, forming a multivesicular body 3: The multivesicular body fuses membrane with a lysosome

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73
Q

What is anchorage dependent

A

When most cells need to be attached to ECM to proliferate and survive

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74
Q

What are the results of the MAPK Pathway

A

Altered proteins

Altered transcription factors

Proliferation due to G1 cyclins being produced (proto-oncogenes)

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75
Q

What is the role of p53

A

Acts as a tumour suppressor

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76
Q

What is one defining characteristic of the EGF Ligand

A

It gets anchored in the plasma membrane due to it containing a hydrophobic domain

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77
Q

What does SDS do to proteins

A

Coats them with a uniform negative charge - masks intrinsic charge. This uniform charge is proportion to the protein’s molecular mass

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78
Q

What causes the polyribosome to be directed towards the ER?

A

The “Signal Sequence” on an already-formed part of synthesising DNA

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79
Q

What differentiates a peptide and a protein

A

A peptide is less than 30 amino acids long A protein is longer

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80
Q

Where do the sidechains of hydrophobic proteins point

A

Point to the outside

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81
Q

What kind of phosphate does a protein kinase add to target proteins? Where does it get this?

A

Adds a gamma phosphate from ATP

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82
Q

Where does folding of proteins take place?

A

In the ER Cisternae.

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83
Q

Where is the site of catalysis in a kinase? How is it regulated?

A

The cleft between each lobe in the catalytic domain is the site of catalysis It is regulated by an activation loop that is phosphorylated to activate kinase itself.

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84
Q

What is Rheumatoid arthritis

A

An autoimmune disease in which your joints become inflamed

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85
Q

What is an E3 ligase? What does it do?

A

E3 ligase is another name for E3 It transfers the ubiquitin from E2 onto the protein

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86
Q

What is one disease that can result from an overactive Wnt pathway

A

Ankylosing Spondylitis

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87
Q

What is the role of proteases in the immune system?

A

Cleaves bits of proteins into correct length to be displayed on MHC molecules

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88
Q

What does a BAX dimer do? Where is it located?

A

Secretes Cytochrome C Located in the mitochondrial membrane

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89
Q

What is a proprotein? What processes does it undergo?

A

A proprotein is an inactive protein. It is activated by the removal of a terminal amino group

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90
Q

What is the function of the aptosome

A

Activates Captase 9 (initiator Captase)

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91
Q

What adds a water molecule to the end of a polypeptide chain in translation?

A

Release Factor

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92
Q

What can unregulated RTK Signalling lead to?

A

Cancer Inflammatory diseases Diabetes

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93
Q

What is the formula for PCR

A

y=a*2^x

y – copy number

a – starting number

x – cycle number

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94
Q

Where is a Conserved Consensus Sequence found? What does it do?

A

Found in the promotor

Binds general transcription factors

Binds specific transcription factors

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95
Q

What is added to the 3’ group on the acceptor arm of tRNA

A

CCA

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96
Q

What are released from when a phosphodiester bond forms DNA bonds

A

Pyrophosphate (PPi) and a Proton

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97
Q

How does beta-catenin act as a transcription factor

A

It binds to TCF

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98
Q

What molecule disrupts the elongation step of translation in all cells

A

Aminoacyl tRNA analogues

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99
Q

What is Lupus Erythematosus

A

An autoimmune disease in which one’s own tissues are attacked

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100
Q

Wat happens in the termination stage of transcription

A

“transcription termination sequence” (polyadenylation signal) signals termination RNA is cleaved 10-30 BPs after RNA polymerase continues to transcribe

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101
Q

What directly activates the MAPK Cascade

A

RAS (Small monomeric G Protein) activated by GEF giving it an ATP

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102
Q

Fundamentally, what regulates apoptosis

A

Caspases

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103
Q

What are the three steps in PCR? What temperatures do they take place at?

A

Denaturisation (95 degrees) - forms single DNA strand Annealing/Hybridisation (55 degrees) - Primer anneals Extension/Elongation (72 degrees) - dNTPs added

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104
Q

How are integins connected to collagen in cell-ECM adhesion

A

Laminin connects Integrins to Collage

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105
Q

What happens to the 3’ end of mRNA

A

polyadenylated

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106
Q

How does one perform 2D gel electrophoresis

A

1: do isoelectric focusing in a tube gel to separate according to charge
2: perform SDS-PAGE on this tube gel to separate according to mass

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107
Q

What is isoelectric focusing (IEF)

A

When you use a gel that has a pH gradient to separate proteins based on their pH

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108
Q

What are the types of Cytoplasmic Tyrosine Kinases

A

SRC

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109
Q

How is the degradation complex prevented from forming when the Wnt ligand is attached to the Frizzled membrane receptor

A

Axin (scaffold protein) binds to LRP GSK (kinase) is inhibited by Frizzled

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110
Q

What are the four diseases that result from too much apoptosis of body cells

A

Alzheimer

Parkinsons L

oss of CD4 cells in HIV/AIDS

Sepsis (apoptosis of immune regulator cells & GIT epithelial cells)

111
Q

What regulates the process of translocation during Translation?

A

Eukaryotic Elongation Factors (EEF’s)

112
Q

What binds to the active site of a protein kinase

A

Protein & ATP

113
Q

What is the core component of the proteasome made of

A

Catalytic (proteolytic) sites

114
Q

What part of the histone can be enzymatically modified

A

N-terminal tails

115
Q

What is adjacent to integrins in the cell-ECM adhesion structure

A

Collagen XVII

116
Q

What is Ubiquitin activating enzyme? What does it do?

A

E1 Forms a bond with ubiquitin

117
Q

What two types of hydrophobic (non-polar) amino acids are ther

A

Aliphathic (chain) Aromatic (ring)

118
Q

What causes phosphorylation of Mitotic Substrates

A

Complexes made of:

  • Mitotic Cyclin
  • CDK 1
119
Q

What splits the plasmid’s DNA or the desired gene’s DNA in protein recombination?

A

Restriction Enzyme

120
Q

What is intrinsic GTPase activity

A

When cells convert GTP to GDP to switch themselves off. Used in G proteins

121
Q

What is PP2B also called? What does it do?

A

A phosphoserine and Phosphotheronine Phosphatase It is also called Calcineurin (binds Ca to get activated)

122
Q

In what types of kinases is the regulatory section part of the same chain as the catalytic domain?

A

Ca Calmodulin Kinase SRC Tyrosine Kinase

123
Q

In which stage of the cell cycle is the signal recieved to replicate

A

G1

124
Q

What happens after protein folding in the processing of newly-synthesised proteins?

A

The protein is enclosed in transport vesicles and budded off from the ER. It then travels to the Golgi for further processing

125
Q

How do effector captases get activated

A

Captase 9 cleaves Procaspases into Effector Caspases

126
Q

What are two RTK receptors used in both the MAPK and PI3K Pathways

A

EGFR

PDGFR

127
Q

What is the main example of a membrane receptor without associated kinase activity

A

G protein coupled receptor

128
Q

What membrane receptor do 50% of modern drugs tarted

A

G Protein Coupled Receptor

129
Q

What are the variable properties that are manipulated in beads that are used in protein purification

A

Affinity for proteins (some won’t stick to beads) Size-exclusion (some proteins will get trapped) Ion-exchange (proteins with opposite charge will stick)

130
Q

If you can’t see a protein after SDS-PAGE, what should you do

A

use a Silver Stain or Coomassie Stain

131
Q

What is VEGF and what role does it play

A

Growth factor Vascular Endothelial Growth Factor. It plays an important role in agiogenesis

132
Q

What are the funcations of the regulatory caps on each end of the proteasome

A

Recognises proteins

Unfolds proteins

Feeds proteins in

133
Q

How does Ca Calmodulin dependent kinase get activated

A

When calmodulin with attached Ca binds to regulatory domain

134
Q

Where does the processing of proteins take place?

A

ER

135
Q

What do viruses do with miRNA

A

Inhibit cellular factors involved in immunity Downregulate expression of viral proteins

136
Q

What are the steps involved in FISH

A

1: Probe and sample prepared
2: Probe labelled
3: denaturing
4: Probe hyybridised to sample
5: sample imaged

137
Q

Which end of the protein does the joining of cadherins occurs

A

N-terminal end

138
Q

What are the specific protein properties that are used for protein purification?

A

Size

Charge

Hydrophobicity

Biorecognition

139
Q

What is the function of the C terminal lobe of a kinase

A

Binds substrate (protein)

140
Q

What causes phosphorylation of G1 substrates

A

Complexes made of: - G1 Cyclin - CDK 2

141
Q

Which molecular family are ICAMs a part of

A

Immunoglobin superfamily

142
Q

What is another name for an enhancer region

A

Regulatory sequence

143
Q

What is the name of the domain in an adaptor protein that links phosphorylated tyrosine amino acids

A

SH2

144
Q

What are the four phases of the cell cycle

A

M

G1

S

G2

145
Q

What keeps adult stem cells from differentiating

A

Intrinsic cell signals Stem cell niche - gives signals to remain as it

146
Q

Describe the outside-in activation of integrins

A

1: Ligands bind to extravellular integrin domain This can result in: 1: The activation of pathways —- such as MAPK 2: These ligands can phosphorylate nearby proteins in cell membrane to create docking sites for other signalling proteins

147
Q

What makes up the degradation complex in the Wnt pathway

A

Axin

GSK

APC

Beta-catenin

148
Q

What are the three sites on a ribosome?

A

E - Exit P - Peptide Bond formation A - Arrive

149
Q

What is the receptor-related protein for that of Frizzled

A

LRP

150
Q

What are the four arms of a tRNA

A

Acceptor Arm (top D arm (right) Anticodon Arm (bottom T, psudouridine, C arm (left)

151
Q

What is the initiation codon at the transcription start site

A

ATG

152
Q

What are the defining characteristics of RTK receptors

A

1: Need to be dimerised 2: Made of groups of Tyrosine Amino Acids

153
Q

What do Dipheria Toxins do

A

modify the EEF-2 in all mammalian cells - Inhibiting translation

154
Q

What are the two regulatory domains of an SRC Tyrosine Kinase called?

A

SH2 & SH3

155
Q

What is one defining characteristic of PDGF

A

It sometimes needs to be cleaved by proteases in ECM to become activated

156
Q

What does malfunctioning of the proteasome pathway lead to?

A

Degenerative diseases such as Alzheimers and Parkinsons Disease

157
Q

What do you see if fish is imaged during metaphase

A

Chromosomes

158
Q

What is the direct role of PI3K

A

Phosphorylates PIP2 to turn it into PIP3

159
Q

Which part of the DNA strand holds nucleosomes together

A

Linker DNA

160
Q

Where does glycosylation happen?

A

ER Golgi Cytoplasm

161
Q

What are four methods of Transfection in protein recombination

A

Electropolation (creates holes by current) Chemicals (Ca salts + Lipids) Microinjection Opticalation

162
Q

What is a Hormone Response Element

A

Short sequence of DNA within promotor of a gene able to bind a specific hormone receptor complex and regulate transcription

163
Q

What makes holes in the mitochondrial membrane enabling cytochrome C to be released? Which secretions do this?

A

Cyototoxic CD8 T cell & NK Cell Release: - Granzymes - Perforin

164
Q

How many domains does an adaptor protein consist of

A

two or three

165
Q

What does rigampicin do

A

antibiotic inhibits a subunit of bacterial RNA polymerase from creasting first phosphodiester bond

166
Q

What is the anti-cancer drug that uses the proteasome pathway to operate? What does it do?

A

Bortezomib Blocks the proteasome - resulting in increased apoptosis of cancer cells

167
Q

What are the two lobes that the catalytic domain of a kinase consists of

A

N terminal lobe C terminal lobe

168
Q

Where are the checkpoints found in the cell cycle

A

G1 and G2

169
Q

What do you see if fish is imaged during interphase

A

nuclei

170
Q

What are the two main anchor proteins in the inside of the cell used in the functioning of a Caderin

A

p-120 catenin beta-catenin

171
Q

What happens to Cytochrome C once it is released into the cytoplasm

A

It joins with APAF and Procaspase 9 to form an Aptosome

172
Q

What is pemiphigus

A

When there are antibodies attached to cadherins of the skin

173
Q

What are the sequences for a stop codon

A

TAA/TAG/TGA

174
Q

What are the two words used when introducing rDNA in Bacteria and Eukaryotes respectively

A

Transformation - Bacteria

Transfection - Eukaryotes

175
Q

How far upstream from the transcription start site is the promotor

A

27 bases upstream

176
Q

What are the two ends of a hydrophilic (polar) amino acid

A

Hydroxyl - positive

Amide - negative

177
Q

Which strand of DNA is not transcribed? What is it called?

A

Coding Strand Sense strand

178
Q

What are the types of Cytoplasmic Serine & Theonine Kinases

A

MAPK

AKT

PKA

PKC

179
Q

How many Restriction Endonuclease sites does an ideal cloning vector have in gene recombination

A

One

180
Q

What happens in initiation of Translation? What regulates it?

A

5’ end of mRNA binds to small ribosomal subunit

Large ribosomal subunit attaches to this

Binding of the Large ribosomal subunit is regulated by Eukaryotic Initiation Factors (EIF’s)

181
Q

What type of amino acid can be phosphorylated?

A

Any amino acid containing a hydroxyl (OH)

182
Q

How many different alpha chains and beta chins are involved in integrins

A

18 alpha chains 8 beta chains

183
Q

What is the first amino acid used in Translation?

A

Met

184
Q

What is a transcription initiator complex

A

Activators (bind to enhancer) and General transcription factors which enable transcription to happen

185
Q

What are the main therapies against the RTK fmaily

A

Trastuzumab: Herceptin (Anti-HER2)

Gefitinib (anti-EGFR)

186
Q

How many base pairs of DNA can a histone wrap

A

147

187
Q

What is a motif? What can it also be called?

A

A specific short amino acid sequence. Also called a Consensus Sequence

188
Q

What are the types of Receptor Tyrosine Kinases

A

EGFR JAK

189
Q

What is autophagy used for

A

Used to break down things INSIDE the cell

190
Q

What can be used as plasmids in protein recombination

A

Plasmids (Extrachromosomal molecules in bacteria) Bacteriophages (viruses that infect bacteria) Cosmids (specialised DNA plasmids with sequences called cos sites)

191
Q

How does PKA get activated

A

cAMP binds to a regulatory subunit

192
Q

What is the role of effector captases

A

Cause celllular proteolysis (protein degradation) which in turn cause cellular apoptosis

193
Q

What processes occur at part of Termination of Translation?

A

1: Stop codon appears in A site
2: Water molecule added to end of polypeptide chain
3: Ribosome subunits dissociate

194
Q

What determines a cell’s fate

A

1: The receptor that a cell has 2: The growth factors that it encounters

195
Q

What type of intracellular filaments are adherens junctions involved with

A

actin filaments

196
Q

What is the polycistronic (many) hairpin loop chain called in RNA interference

A

Pri-miRNA

197
Q

How do small monomeric G proteins activate kinases? Where do they get their energy to do this?

A

Bind GEF (Gaunine nucleotide exchange factor) In the process, use GTP.

198
Q

What is the role of PIP3

A

Binds AKT (using it’s PH domain) which enables other enzymes to phosphorylate AKT

199
Q

What happens to AKT once it is phosphorylated

A

Acts as a kinase and phosphorylates proteins (NOT TRANSCRIPTION FACTORS) involved in survival and proliferation

200
Q

What is the DNA sequence of a splice site

A

AG/…exon…/GT

201
Q

What is the role of intermediate filaments

A

Provide mechanical strength for the cell

202
Q

What is used as a solvent that proteins can run through in the process of protein purification

A

Beads with specific properties

203
Q

What is PP2A

A

A Phosphoserine and Phosphotheronine Phosphatase. It reverses phosphorylation in signalling pathways activated by growth factors

204
Q

What is the collective term for a base and sugar

A

nucleoside

205
Q

What is the name of the process whereby sugar groups are added to a newly-synthesised protein

A

Glycosylation

206
Q

What are some examples of adult stem cells

A

Intestinal villus Muscle satellite cell Hair follicle Haematopoeitic stem cells

207
Q

What is the role of Actin filaments

A

Determine the shape of the cell’s surface

Responsible for locomotion

208
Q

In what types of kinases is the regulatory section part of a different protein chain as the catalytic domain

A

PKA CDK

209
Q

Describe the process of Microautophagy

A

When endogenous proteins (inside the cell) get endocytosed into lysosome of cell

210
Q

What is the primary role of the enhancer

A

To control the rate of the promotor activation

211
Q

What is pemphigoid

A

When there are antibodies attached to components of the hemidesmosome

212
Q

What causes the cell to proceed from the G1 phase into the S phase?

A

Phosphorylated G1 substrates

213
Q

Which two proteins of the Wnt pathway are scaffold proteins

A

Axin and APC

214
Q

How is Beta-catenin degraded when there is no ligand attached to the Frizzled membrane receptor protein

A

GSK causes beta-catenin to become phosphorylated which causes it to be ubiquinated by E3 Ligase

215
Q

What makes it possible for there to be many more mRNAs than genes?

A

Alternative splicing - many different ways an mRNA can be spliced

216
Q

What does RNA Polymerase attach to

A

Transcription factors at the promotor

217
Q

What is one disease that can result from an overactive Wnt pathway

A

Ankylosing Spondylitis

218
Q

What is the active form of the G Protein? Vice versa?

A

Active = GTP on alpha subunit Inactive = GDP on alpha subunit

219
Q

In PAGE, how is the migration distance of the protein related to it’s mass

A

The migration distance is negatively proportional to the log of its mass

220
Q

Describe the process of Macroautophagy

A

1: Phagopore surrounds large cellular components of cell 2: Phagopore closes to form Autophagosome 3: Autophagosome fuses membrane with lysosome

221
Q

What is the significance of the restriction point? Where is it found in the cell cycle?

A

Once past restriction point, cells are committed to divide Restriction point happens late in the G1 phase

222
Q

When do proteins stop moving in IEF

A

At their Isoelectric point. This is when the Isoelectric Charge is equal to their pH

223
Q

What is the pH gradient in IEF caused by?

A

Presences of ampholytes in IEF gel causes pH gradient

224
Q

What process regulates degradation of proteins in the proteasome?

A

Polyubiquination

225
Q

What is the sequence of amino acids that integrins always bind to

A

RGD: - Arganine - Glycine - Aspartic Acid

226
Q

What is the chemical modification that rRNA undergoes to become a ribosome

A

Methy groups added Pseudouridine added

227
Q

Which are the signalling pathways that are involved with regulating growth factors

A

Tyrosine Kinase Receptor Pathways (MAPK, PI3-K)

228
Q

What is a directly labelled probe in fish called

A

fluorophore

229
Q

What constitutes the tertiary level of protein structure

A

3D structure of a chain

230
Q

What happens to Procaspase 8 when the death receptors are active

A

The activated death receptors cause Procaspase 8 to be cleaved into Initiator Caspase 8

231
Q

What are transient amplification cells?

A

Cells that give rise to other differentiating cells (like stem cells) but that differentiate themselves later on into the desired tissue

232
Q

How does phosphorylation of a protein result in conformational changes

A

Phosphorylation adds two negative charges which changes the protein’s structure

233
Q

Which end of the Amino Acid is added to tRNA? What regulates this?

A

COOH group - added to 3’ end tRNA synthases

234
Q

What happpens when a scaffold protein is phosphorylated?

A

Many different proteins with SH2 domains are recruited

235
Q

Which is the length-determining phase of the cell cycle

A

G1

236
Q

What causes translation suppression of mRNA

A

When the miRNA does not match perfectly

237
Q

What happens to the 5’ end of an mRNA

A

Capped with 7-methyguanosinetriphosphate

238
Q

What causes degradation of mRNA

A

When the miRNA matches perfectly

239
Q

What happens in the Initiation stage of transcription

A

– Helicase, a subunit of RNA Polymerase, unwinds DNA

– First 8/9 nucleotides are linked

– Transcription factors and RNA polymerase are released from the promotor region and RNA polymerase moves along

240
Q

How is the sample prepared during FISH

A

Cells are fixed (formaldehyde) and Permeabilised (detergents)

241
Q

What are the four required features of a cloning vector in protein recombination

A

1: Appropriate origin of replication 2: Marker genes 3: Restriction endonuclease (ER) sites 4: Promotors

242
Q

In which way does one label condons or anticodons?

A

3’ to 5’

243
Q

What determines the speed of migration of proteins in PAGE?

A

Molecular weight

244
Q

What amino acid does PKA phosphorylate

A

Serine and Threonine

245
Q

What is the function of effector enzymes

A

To produce second messengers (e.g. cAMP, IP3)

246
Q

How is an SRC Tyrosine Kinase activated

A

Dephosphorlatioon

247
Q

How is the probe prepared during FISH

A

DNase I - Introduces Nicks into probe DNA Polymerase - Fills in nicks with modified dNTP

248
Q

What does Actinomycin D do

A

antibiotic Inserts between two GC pairs in DNA (prokaryotic and eukaryotic)

249
Q

What do scaffold proteins do

A

Bind other proteins to bring them into a complex

250
Q

What is Ubiquitin-conjugating enzyme? What does it do?

A

E2 Recieves ubiqutin from E1

251
Q

What are the Pyrimidine Bases

A

C, T and U

252
Q

What kinase is a cytokine receptor associated with

A

JAK (tyrosine kinase) that phosphorylates the tail-end motif sequence containing Tryosine

253
Q

What are the two functions of adaptor proteins

A

Link proteins together Pass signals on

254
Q

What are the three classes of RNA Polymerase

A

Type 1 - makes rRNA

Type 2 - makes mRNA

Type 3 - makes tRNA

255
Q

What is used to prepare for viewing the product of PCR

A

Agarose Gel Electrophoresis

256
Q

What are the sequences found in the promotor region

A

TATA CAAT

257
Q

What part of the Golgi does a transport vesicle containing a newly-synthesised strand of protein attach to?

A

The cis face

258
Q

What are the types of Receptor Serine & Theonine Kinases

A

Transform growth factor beta

TGFBRI

TGFBRII

259
Q

What is the function of GSK

A

Kinase that acts on beta-catenin in the degradation complex of the Wnt Pathway

260
Q

What process regulates protein sorting (making sure proteins get transported to correct location)

A

Monoubiquination

261
Q

Which part of DNA is transcribed? What is it called?

A

Template Strand Antisense Strand 3’ —–> 5’

262
Q

In PAGE, what does a lower concentration of acrylamide result in?

A

Bigger pores

263
Q

What is the role of microtubules

A

Determine position of organelles

Directs intracellular transport

264
Q

What is the most common cancer as a result of not enough apoptosis

A

Lymphoma

265
Q

What type of intracellular filaments are desmosomes involved with

A

Intermediate filaments

266
Q

What type of polymerase is used in PCR

A

Taq Polymerase

267
Q

Which molecules are involved with the folding of proteins

A

hsp60 protein-like complex GroES Cap

268
Q

What constitutes the primary level of protein structure

A

Peptide bonds between amino acids, making a chain

269
Q

What prevents two BAX proteins binding to each other? How does it do this?

A

BAX binds to BCL2, preventing it from binding to another BAX

270
Q

In the G Protein, which subunit dissociates and regulates the target protein

A

Alpha subunit

271
Q

Describe the structure of a kinase

A

A polypeptide chain that has -Catalytic domain (with active site) -Regulatory domain A polypeptide chain with a regulatory subunit

272
Q

What two processes regulate chromatin organisation

A

methylation and acetylation

273
Q

Which molecule undergoes proofreading activity? What is this activity called?

A

DNA Polymerase Exonuclease activity

274
Q

What is the function of reverse transcriptase? What is it used for?

A

Reverse transcribes mRNA into DNA. It is used to take an mRNA molecule and change it into it’s corresponding DNA strand to insert it into a recombinant plasmid

Molecular Medicine (3 decks)

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