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BIOL*1090 > Midterm 2 > Flashcards

Midterm 2 Flashcards

1
Q

What does it take to make a cell? 

A
  1. Information (dna & rna)
  2. Chemistry
  3. Compartments
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2
Q

Eunucleation 

A

Mechanism by which maturing red blood cells reject the nucleus during differentiation 

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3
Q

Differentiation

A

The process of developed mint during which cells of multicellular organisms become specialized information, is important to make cell and create different specific cell types 

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4
Q

Miller Urey experiment

A

In 1952 chemical experiment that stimulated conditions thought to exist on early earths, and to test the chemical origin of life under those conditions 

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5
Q

Operons and haldaries primordial soup hypothesis

A

Putative conditions on primitive earth, favourite chemical reactions that made more complex organic compounds from simpler organic compounds 

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6
Q

Abiogenesis 

A

Chemical origin of life, organic compounds plus energy in the form of electricity and UV produce simple organic compounds 

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7
Q

First group of intermediate products from abiogenesis 

A

Formaldehyde, hydrogen cyanide 

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8
Q

Second group of intermediate products in abiogenesis 

A

Urea, formic acid and amino acids 

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9
Q

Conclusion of abiogenesis experiment 

A

Amino acids can be generated in conditions to mimic those of earlier during later experiments showing that other chemical reactions can generate simple sugars. The base is found in nucleotides and lipids needed to form primitive membranes. 

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10
Q

 Compartments

A

Single or double lipid layer, membrane, examples, including mitochondria, chloroplast cell nucleus 

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11
Q

Roles of compartments 

A

Establish physical boundaries that enable cells to carry a different metabolic activities, generate a micro environment, especially temporarily regulate biological process 

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12
Q

Who discovered sell an early microscope

A

Robert Hooke 

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13
Q

The cell theory 

A

By Matthias, Jacob show Leiden and Theodore Schwann
1. All living organisms made of one or more cells
2. Cell is the most basic unit of life.
3. All cells arise, only from pre-existing cells 

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14
Q

Basic properties of cells 

A
  1. Highly complex and organized
  2. Activity controlled by a genetic program.
  3. Can’t reproduce and make copies of themselves
  4. Assimilate and utilize energy
  5. Carry out many chemical reactions
  6. Engage in mechanical activities.
  7. Respond to stimuli
  8. Capable of self regulation,
  9. Evolve 
    
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15
Q

Prokaryotes

A

Include bacteria, and archaea
were the only form of life, millions of years ago
single celled organism
1 to 10 µm
have no nucleus or organelles ribosomes are present but small reproduce asexually
genetic material is found in nucleotide in a circular fashion plasmid 

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16
Q

Eukaryotes 

A

Protozoa are single celled, eukaryotes, fungi, plants, and animals
Eukaryotic cells are found in multicellular organisms, but can be unicellular to
size is 10 to 100 µm
has a nucleus and organelles ribosomes are large
genetic materials found in nuclear compartment and arranged as chromosomes 

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17
Q

Difference btw Animal and plant cells 

A

Animal cells have lysosomes and microvilli and plant cells do not
Plant cells have cell walls, vacuoles, chloroplast, and plasmodesmata and animal cells do not 

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18
Q

Viruses 

A

macromolecular packages that function and only reproduce within living cells/host are not considered to be cells or alive but have four of the nine basic properties of cells

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19
Q

What 4 properties of cells do viruses have? 

A

They are complex evolve, genetic controlled, can reproduce (only within a host)

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20
Q

Virion

A

A virus that exists outside of a host made up of small amount of DNA and RNA that encodes hundreds of genes 

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21
Q

Bacteriophage 

A

Virus that infects and replicate within bacteria and archaea has a capsid head DNA a collar sheet and is the Victor cookie monster robot has a spikes, a tail and a base plate 

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22
Q

Two main types of viral infection 

A

Lytic and nonlytic 

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23
Q

Lytic

A

Production of virus particles ruptures and kills cells. Example influenza. 

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24
Q

Non-lytic 

A

Also known as integrative, or lysogenic, infected cells can survive often with impaired function 
Viral dna is inserted in host genome

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25
Q

Provirus

A

Viral dna is inserted in host genome

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26
Q

How do viruses work? 

A

Once inside a cell viruses hijack cellular machinery to synthesize, nucleic, acids and proteins, as parts are than assembled to make new virus particles to infect other cells 

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27
Q

Virus life cycles

A

1- virions attach to host cell
2- virion penetrates cell and its dna is uncoiled
3- early transcription- enzymes are synthesized
4- late transcription- dna is replicated
5- late transcription - capsid proteins are synthesized
6- vitions mature
7- virions are released

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28
Q

5 genes encoded by rna genome

A

Phosphoprotein, matrix protein, glycoprotein and viral rna polymerase

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29
Q

How do rna vaccines work

A

By tricking the body cells into producing a fragment of a virus, an antigen from an RNA template

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30
Q

Strategy to make homemade vaccines at a lower dose 

A

In corporate instructions for making replicase, which can make lots of copies of RNA template producing antigens 

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31
Q

Function of plasma membranes 

A

1- define cell boundary
2- define enclose compartments
3- control movement of material into and out of cell
4- allow response to external stimuli
5- enable interactions between cells
6- provide scaffolds for biochemical activities

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32
Q

Structure of plasma membrane

A

Trilaminar
Made of phospholipid bilayer
6nm thick
Hydrophilic phospholipid heads exposed to either fluid and hydrophobic tails are buried

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33
Q

Amphipathic mlc

A

Mlc that have both hydrophobic (non-polar) and hydrophilic (polar) regions
Ex. Phospholipids

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34
Q

Where does Phospholipid synthesis occur

A

Occurs in the cytosol and outer endoplasmic reticulum membrane, which is all the molecular machinery for synthesis and distribution multi step process 

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35
Q

Steps of phospholipid synthesis 

A

1- in cytosine fatty acids are attached by attachment of coA mlc
2- the activated fatty acids bond to glycerophosphaye and are inserted into cytosolic leaflet
3- the phosphate is removed by a phosphate enzyme
4- choline already linked to phosphate is attached via choline phosphotransferase
5- flippase transfer some of phospholipids to other leaflet

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36
Q

Choline

A

Head group of phospholipid

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37
Q

Choline phosphotransferase

A

Integral protein/enzyme that gives head to phospholipid

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38
Q

The fluid mosaic model of biological membranes 

A

Proposed by Seymour, Jonathan Sigur and Garth Nicholson in 1972
Plasma membrane is viewed as a two dimensional liquid that restricts the diffusion of membrane components dim, different proteins are embedded in the phospholipid by layer. Components are mobile and components can interact 

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39
Q

Dynamics of plasma membrane 

Lipid movement

A

Lipids move easily within leaflet, but the lipid movement from one leaflet to another, is difficult and slow 

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40
Q

Dynamics of plasma, membrane protein, movement 

A

Membrane proteins diffuse within the bilayer
movement of proteins is restricted rapid movement especially limited. Long range. Diffusion is slow. 

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41
Q

Fryc edidn experiment

A

Fused, blue mouse surface, pro Tien, cell and green human surface broken sell through forced sell diffusion, and after a short period of time the surface proteins of both cells defuse around the unified membrane and mingle rather than being locked in original location 

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42
Q

Properties of membranes 

A

Membranes are approximately 6 nm thick. They are stable, flexible and capable of self assembly.

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43
Q

Three classes of membrane proteins 

A

 Integral
Peripheral
Lipid anchored 

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44
Q

Integral proteins 

A

Membrane proteins, span, lipid bilayer 

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45
Q

Integral proteins functions 

A

One transport of nutrients and ions
2. Cell to cell communication gap junction,
3. Attachment, example skin cells attaching to body 

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46
Q

Difference between outer leaflet and inner leaflet 

A

Biological membranes are asymmetrical
Outer- glycolypids and glycoproteins
Less dynamic
Inner more dynamic, less cholesterol
Involved in vesicle formation

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47
Q

Fluidity of biological membranes

A

Temperature is an important variable of fluidity fluidity is crucial to function 

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48
Q

Warming of membrane,  

A

Increases fluidity liquid crystal 

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49
Q

Cooling of membrane 

A

Decreases fluidity 

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50
Q

 Unsaturated lipids

A

Increase fluidity 

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51
Q

Saturated lipids 

A

Reduce fluidity 

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52
Q

How can lipid composition of membranes be changed in response to temperature changes? 

A

One. Desaturation of lipids
To exchange of lipid chains . 

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53
Q

Why is balance between ordered rigid structure and disordered structure important 

A

Allows mechanical support and flexibility, membrane assembly, and modification and dynamic interactions between membrane components. Example proteins can come together reversibly 

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54
Q

How does cholesterol affect fluidity of biological membrane? 

A

Cholesterol modulate membrane, fluidity it, accessible by directional regulator of membrane, fluidity because high temperatures, it stabilizes the membrane and raises the melting point, whereas as low temperature is it in circulates between the phospholipids, and prevents them from clustering together and stiffening
It ultra the packaging and flexibility of lipids if added to a liquid crystal membrane, fluidity decreases, if added to a crystalline gel, membrane fluidity increases 

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55
Q

Transmembrane protein domain 

A

A peptide sequence that is largely hydrophobic and charged and spins across the plasma membrane
It permanently attaches the protein to the plasma membrane


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56
Q

What is the most common protein structure element crossing biological membranes? 

A

The alpha Helice

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57
Q

What are the nine amino acids with hydrophobic side chain? 

A

Lysing alanine, failing leucine Prolene phenylalanine methionine and tryptophan 

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58
Q

Tetraspanins

A

A family of membrane proteins found in all multicellular eukaryotes 
Have four transmembrane, alpha helices, and two extra cellular domains, one short, and one longer some Tetris pendants can be glycosylated on extracellular Loop 

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59
Q

Function of tetraspanins

A

Play a role in adhesion, motility, proliferation and more 

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60
Q

Four basic mechanisms of moving molecules across membranes 

A

1) simple diffusion (passive)
2) diffusion through a channel (passive)
3) facilitated diffusion (passive)
4) active transport (active)

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61
Q

Simple diffusion 

A

Is down a concentration gradient, (high concentration to low concentration)
works for very small on charge molecules like oxygen and carbon dioxide  (not water)

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62
Q

Diffusion through channels 

A

A form of passive transport,
effective for small charged molecules ions like Na+ K+ Ca2+ Cl-
Ions move down a concentration gradient
channels are selective only allowing particular ions to pass,
formed by integral membrane proteins,
typically subunits that line an aqueous pore

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63
Q

Ion channels

A

Can be open or closed important to provide channel with ability to respond to different stimuli. Example neurotransmitters can be turned on or off two types voltage gated, and ligand gated.

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64
Q

Two types of ion channels

A

Voltage gated and ligand gated

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65
Q

Voltage gated ion channel

A

 Example, sodium and potassium ion channels some channels can respond to changes in charge across membrane

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66
Q

Ligand gated channels 

A

Ion channels like acetylcholines receptor that respond to finding of specific molecule on its surface a ligand binding of a ligand produces confirmational change in structure of receptor/channel

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67
Q

Ligand

A

Molecule that binds to an ion channel to change its confirmation

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68
Q

Toxins, targeting ion channels

A

Tetroxin, TTX
Curare

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69
Q

Tetroxin

A

is a potent neurotoxin from puffer fish that blocks sodium ion channel and inhibits the firing of action potential by neurons prevents nervous system from carrying messages to muscles, including the diaphragm which causes death via respiratory failure

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70
Q

Curare

A

 Is a toxin targeting ion channel that’s a mixture of organic compounds found in different plant originating from South America. It’s used as a paralyzing poison and hunting tool. It’s a competitive antagonist of nicotinic acetylcholine receptor and occupies the same spot on the receptor, as acetylcholine with greater affinity and elicits no response, it’s a non-depolarizing muscle relaxant

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71
Q

Facilitated diffusion 

A

Compound binds specifically to integral membrane proteins, called facilitated transporter, change in transport conformation allows the compound to be released on other side of membrane compound moves down a concentration gradient
Example is of carriers are glucose transporters and symporter and anti-Porcher

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72
Q

Glucose transporters

A

Type of facilitated transport,
Most animals import glucose down a concentration gradient, via this facilitator
1 transport is ready to accept the glucose molecule
2) glucose is accepted by transporter. 3) intracellular site of transporter opens
4) glucose is released, and the cycle repeats.

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73
Q

Na+ & glucose Symporter

A

A carrier facilitated transport
Cells need to move substances from a low concentration to high concentration. Examples of the reabsorption of glucose in the kidney in this case cells can’t rely on a concentration gradient, so they rely on the chemical gradient of another molecule that will not reach extracellular and intracellular equilibrium in this case is sodium .

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74
Q

Na+ and glucose symporter steps

A

1) simultaneous binding of two sodium ions, and one glucose to the transporter with outward facing binding sites
2) this causes a confirmation change in the transporter occluded
3) eventually the transporter adopts an inward-facing confirmation that allows
4) the dissociation of the two sodium molecules to the cytosol and as a result, the glucose molecule gets pushed in as well
5) return of the outward facing confirmation to repeat the cycle

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75
Q

Anti-Porter

A

A third type of carrier for facilitated transport concentration of gradient of one molecule is used to transport other molecules in opposite directions. An example is sodium protein exchanger in the nephron of the kidney this anti-porter transports sodium ions into the cell and protons out of the cell is responsible for maintaining pH and sodium levels in specific kidney cells

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76
Q

Active transport

A

Compound binds specifically to integral membrane protein called active transporter
 Change in the conformation of the transfer caused by the hydrolysis of an ATP molecule allows molecules to be released on other side of the membrane using this mechanism compounds can move across a concentration gradient. It requires energy in the form of ATP molecules.

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77
Q

Na+/K+ pump

A

ATPase maintains cellular, sodium and potassium concentration using ATP. three sodium ions exit the cell and two potassium ions Enter for each ATP molecule hydrolyze commonly referred to as the NA plus/K plus pump.

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78
Q

 Why is the sodium potassium pump important

A

It’s important to maintain concentration of sodium ions outside than inside the cells cells spend energy to achieve and sustain the sodium chemical gradient required for nonstop activity of the sodium glucose symporter

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79
Q

How is cell size maintained

A

 Through active transport
Hypertonic—> shrunk
Hypotonic —> swollen
Isotonic—-> normal
Lysed—> very hypotonic, bursting

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80
Q

Transmembrane, proteins and signal transduction

A

Transmembrane proteins play a big role in signal transduction as they convert extra cellular signal into intracellular signal signal transduction allows cells to rapidly respond to events happening in their environment, such as grow survive, differentiate move

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81
Q

Ligand

A

Small molecule that binds to receptors like in binding changes. Confirmation of the receptor proteins ligand does not enter the cell confirmation change causes other proteins inside of cell or membrane to become activated.

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82
Q

Three stages of signal transduction

A

1) binding of ligand to receptor
2) signal transduction via second messengers like cAMP, calcium or G-protein
3) cellular response- cellular growth, division, store of glucose molecules as glycogen

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83
Q

Examples of disease caused by defect in signal transduction

A

Cancer, diabetes, different brain disorders

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84
Q

Glycogenolysis

A

A type of signal transduction, how epinephrine a.k.a., adrenaline activates conversion of glycogen stored in the liver to glucose

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85
Q

Glycogen molecule

A

Glycogen in protein is surrounded by branches of glucose units
Glycogen is an enzyme that acts as a primer to polymerize the first glucose molecule then other enzymes take over

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86
Q

What enzyme releases glucose units?

A

Phosphorylase P

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87
Q

Role of anchor proteins in the cellular matrix

A

Anchor, proteins, playing important role in interacting with components of the extracellular matrix
Are ECM is abundant in connective tissues of animals

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88
Q

ECM

A

Extracellular matrix is an organized network of material produced and generated by cells
The outside of cells

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89
Q

Functions of ECM

A
  1. Cell adherence
  2. Communication between cells.
  3. Cell shape, mechanical support, and structural integrity.
  4. Serves as barrier filters out some particles.
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90
Q

Extracellular matrix and ageing wrinkles

A

Wrinkles are caused by fibrosis of connective tissues of the skin fibrosis is scarring and thickening. They develop from inquiry, extra pairs of injured elastin, fibers, and collagen fibers.

91
Q

Components of the extra cellular matrix

A

Proteins like collagen, glycoproteins proteoglycans

92
Q

proteoglycans

A

Proteins with chains of poly saccharide’s

93
Q

Cell walls

A

Are cells of bacteria, plants and fungi have walls that act as the extra cellular matrix. They are composed of cellulose, hemicellulose pectin, and

94
Q

Cell wall function

A

provide structural support to cells and proteins equivalent to skeleton protect the cell from mechanical damage and pathogen attacks.

95
Q

function of the cytosol

A

Protein synthesis, many metabolic pathways and ribosome assembly

96
Q

Function of the nucleus

A

Contains genome, DNA and site of RNA synthesis

97
Q

Function of the ER

A

Synthesis of lipids and proteins

98
Q

Function of the Golgi apparatus

A

Protein, modification, packaging of proteins and lipids

99
Q

Functions of lysosomes

A

Degradation of cellular material

100
Q

Function of endosomes

A

Sorting and recycling

101
Q

Function of mitochondria

A

ATP synthesis and apoptosis

102
Q

Chloroplast function

A

Photosynthesis ATP synthesis

103
Q

Peroxisome’s function

A

Oxidation of toxic materials

104
Q

Endo symbiotic theory

A

Sim biogenesis the theory of the origin of a eucaryotic cells from prokaryotic organisms. Siri holds that organelles in eucaryotic cells evolved through symbiosis of individual single celled prokaryotes symbiosis means living together close and long-term biological interaction theory holds that organelles with two membranes, like mitochondria and chloroplasts represent formerly free, living, prokaryotes, taken one inside the other.

105
Q

Endo symbiotic, Siri evidence

A

One binary fission of mitochondria and plastids
2circular DNA inside these organelles similar to bacteria

106
Q

Aerobic respiration

A

Converts in presence of oxygen energy, stored in food molecules glucose into chemical energy, stored in ATP this process produces carbon dioxide as a byproduct

107
Q

Photosynthesis

A

Builds carbs, using energy from sun and carbon dioxide also produces oxygen

108
Q

Outer mitochondrial membrane

A

Contains many enzyme with diverse, metabolic functions. Example monoamine oxidase is breakdown. Monoamine neural transmitters has porrins

109
Q

Porrins

A

Large channels, permeable passive diffusion to many molecules when opened such as ATP and sucrose

110
Q

Inner mitochondrial membrane

A

High protein to lipid ratio, 3 to 1 double layer, folds, called Christy, increase surface area and contain machinery for aerobic respiration and ATP formation rich in phospholipid called cardiolipin

111
Q

Cristae

A

A double ear falls that increase membrane surface area and contain machinery for aerobic respiration and ATP formation

112
Q

Cardiolipin

A

Characteristic of many bacterial membranes, and needed for optimal function of many enzymes

113
Q

Aqueous compartments mitochondria has two

A

One intermembrane space

2) mitochondrial matrix
high protein, Contant gel like consistence space containing mitochondrial, ribosomes and DNA in mammals,

114
Q

How many genes does mitochondrial dna encode

A

mitochondrial DNA and codes 37 genes

115
Q

Photosynthesis two parts

A

Light dependent reaction and light. Independent reaction also known as Calvin cycle.

116
Q

Light dependent reaction

A

Occurs in the thylakoid membrane chlorophyl in light harvesting complex electrons enter etc. Also in thylakoid membrane H plus is pumped into the silo quite a lumen. ATP and NADPH are made in the light reaction and are used to make carbohydrates in the light independent reaction.

117
Q

Light independent reaction

A

Occur in the stroma of chloroplasts ATP and NADH pH make a light reaction used to make carbohydrate reduction of carbon dioxide to form carbohydrates

118
Q

Apoptosis

A

Programmed cell death, a normal process that involves the death of cells in a coordinated sequence of events. Part of an organisms, growth and development. Example is inter-digital Seldes leading to the regression of soft tissue between embryonic digits in many vertebrates.

119
Q

Apoptosis characteristics

A

Cells undergoing apoptosis show shrinkage,
blebbing, bulge or Protrusion of plasma, membrane fragmentation of DNA and nucleus loss of attachment to other cells, and engulfment by phagocytosis

120
Q

Are intrinsic pathway of apoptosis

A

Initiated by intracellular stimuli like genetic damage, hypoxia and virus

121
Q

BAX proteins

A

Killer proteins that cause change in the mitochondrial membrane and lead to leakage of cytochrome C

122
Q

Apoptosis steps

A

BAX killer proteins, cause change in mitochondrial membrane and lead to leak of cytochrome C backs assembles on the outer mitochondrial membrane to form pores which release cytochrome C release of apoptonic mitochondrial proteins commits a cell to apoptosis cytochrome C assembles apoptosomes in cytoplasm
Apoptosomes activate executioner caspases which disrupt cell adhesion, destroy lamins blah blah

123
Q

Caspases

A

Product in apoptosis which disrupt cell adhesion destroy nuclear filament breakdown cytoskeleton activate genome break down

124
Q

Disease related to apoptosis

A

Cancer is caused by too little apoptosis and malignant cells do not die. Alzheimer’s is caused by too much apoptosis as with many degenerative diseases.

125
Q

polarized structure of a secretory cell

A

Synthesized in the rough endoplasmic reticulum processed in the end of plasmic reticulum further processed in the Golgi, concentrated in vesicles, delivered to plasma membrane for secretion

126
Q

Mucin

A

Secreted, protein, glycoprotein component of mucus

127
Q

GFP

A

Green Fluorescent protein
from jellyfish
can be fused with cellular proteins fusion protein can be expressed in cells observations of this provide info on Endo Genesis proteins

128
Q

I vesicular transport/trafficking

A

Transport of materials between compartments can be from organelle to plasma, membrane and vice versa or between organelles uses transport vesicles

129
Q

Transport vesicles

A

Small spherical membrane, enclosed organelles that but off donor compartments infused with acceptor or recipient compartments

130
Q

Target movement directed

A

Uses cytoskeleton and motor proteins,
sorting signals recognized by receptors

131
Q

Key elements of vesicular transport

A

1) movement of vesicles uses cytoskeleton and motor proteins can be anterior grade or retrograde
2) tethering vesicles to target compartments via proteins from rAB family
3) docking of vesicle uses proteins, called snares snare assembly provides energy for fusion
4) fusion of vesicle and target membrane

132
Q

Exocytosis

A

Vesicle travels from organelle to plasma membrane
ER to Golgi to plasma membrane
Anteriograde movement

133
Q

Endocytosis

A

Vesicle travels from Plasma membrane organelle
Plasma membrane to Golgi to ER
Retrograde transport

134
Q

Rough endoplasmic reticulum

A

Has many ribosomes proteins synthesis by many of these ribosomes

135
Q

Smooth ER

A

Lacks ribosomes, primary site of lipid synthesis

136
Q

Functions of the
Smooth ER

A

1) lipid synthesis,
2) production of steroid hormones,
3) detoxification 
4) sequestration/storage of calcium 2+ ions

137
Q

Intracellular calcium handling

A

Cells invest significant number of energy to controls changes in calcium 2+ concentration

138
Q

Why is calcium 2+ excluded from cytosol

A

Ca2+ does not bind water well, which will precipitate phosphates and make proteins insoluble so calcium in cytosol is handled

139
Q

Calcium 2+ in cytosol…

A

Sound by range of calcium binding proteins
Forced through pumps and transporters
Sequestered into specific organelles, like the smooth ER

140
Q

Functions of rough ER

A

1 synthesis of membrane phospholipids
2 glycosylation of proteins addition of carb to specific protein chain
3 protein, folding quality control involves activity of molecular chaperones, a specific type of proteins that assist in the folding process
4. Proteins synthesis, modification and transport of proteins targeted to ER targeted to other endomembrane compartments.

141
Q

Endoplasmic reticulum

A

Compartment of flattened, sacs, and tubules

142
Q

Where does all protein translation begin?

A

Translation is RNA to polypeptide, and all proteins. Translation begins on free ribosomes in cytoplasm . Translation is completed in one of two ways either on free ribosomes or ER bound ribosomes

143
Q

Proteins translated completely on free ribosomes

A

Cytosolic proteins, peripheral membrane, proteins proteins, targeted to the nucleus, mitochondria peroxosomes chloroplasts 

144
Q

If polypeptides don’t have a signal peptide, where do they go?

A

To cytosol

145
Q

If polypeptides have an amino terminal signal, where do they go?

A

To chloroplast or mitochondrion

146
Q

If polypeptides have an internal signal, where do they go

A

To the nucleus

147
Q

Proteins completely translated on ER bound ribosomes

A

Secreted proteins, integral membrane proteins, soluble proteins associated with inside the lumen of Endo membrane system (proteins that function within the ER Golgi and lysosomes)

148
Q

Endo membrane system

A

Comprises the ER, Golgi apparatus and lysosomes

149
Q

Co translational import

A
  1. SRP signal recognition particle binds to signal sequence and stops the translation process
  2. SRP binds to SRP receptor to target hole translation complex to ER
  3. SRP is released and ribosome binds to translocon once done, protein synthesis, resumes.
  4.  Polypeptide enters ER through translocon, and is translated
    in the end The signal peptide is reeved off and chaperoned folds the protein.
150
Q

Proteins targeted to the mitochondria

A

The TOM complex is equivalent to the SRP complex and translocon

151
Q

Endocytic pathways of protein sorting

A

Protein targeted to the ER lumen after fully Maiden properly fold it has one of two options
1) retained in the ER lumen if that is where it functions
2) it is transported from the ER to Golgi complex for further modifications, and then delivered to distal parts of the biosynthetic secretory pathway in some cases for another sensation could be outside of the cell example secreted hormones like mucin

152
Q

Peroxisome

A

Organelle known as micro body found in all eucaryotic cells involved in a small number of enzymatic reactions,

153
Q

Small number of enzymatic reactions that peroxisome’s are involved in

A

catabolism of long chain fatty acids reduction of reactive, oxygen species, and biosynthesis of plasmologens

154
Q

Zellweger syndrome

A

No peroxisome’s made due to mutation in paroxysm assembly factor one autosomal recessive disorder that causes severe brain development defects. Patient usually doesn’t survive beyond one year.

155
Q

Cystic fibrosis

A

Caused by mutation in CFTR causes degradation in ER of CFTR protein fails to reach the surface or other sites

156
Q

Synthesis of integral membrane

A

Part of polypeptide enters cell
part stays within full phospholipid membrane
part leaves
N terminal signal sequences, direct proteins to their respective organelles once they arrive, other intrinsic sequences within proteins, direct them to the correct compartment or membrane

157
Q

Three parts of the Golgi apparatus

A

Trans golgi network - near surface
Medial Golgi -in middle
Cis Golgi - closest to er (proximal)

158
Q

Structure of Golgi complex

A

Smooth flattened disc like sister name eight or if you were sister in a stack range from a few to several thousand stacks per cell curved like shallow bowl
Shows, polarity, sis, medial, trans cisternae

159
Q

Cis golgi networks

A

And acts as a sorting station sorts weather proteins should continue back to next Golgi station or go back to the ER

160
Q

Trans. Golgi net work.

A

Sorts proteins into different types of vesicles, which go to plasma, membrane or other intracellular, destinations, example, lysosomes, proteins are modified stepwise as they traverse the Golgi

161
Q

Golgi apparatus

A

Processing plant of the cell fully processed proteins are exported to the trans Golgi Nettwerk, and then sorted and delivered to their final destinations

162
Q

Coat proteins

A

Help vesicles from the ER travel to the Golgi in between the Golgi sub compartments
Include COP 1 and COP II

163
Q

Functions of coat proteins

A
  1. Help form the vesicle.
  2. Help select cargo material inside or on vesicle.
164
Q

Constitutive, secretory pathway

A

Secretary vesicles can go to exocytosis without security

165
Q

Regulated, secretory pathway

A

Secretary granule is regulated takes more time example the release of insulin and neurotransmitters

166
Q

Coatomer

A

Cop 1 and 2
Protein complexes that assemble on the cytosolic surface of donor compartments at sites where budding takes place

167
Q

COP I

A

Coded vesicles move in retrograde direction

168
Q

COP II

A

Coded vesicles move an anterior grade direction

169
Q

Key features of lysosomes

A

Digestive organelles
25 nm to 1 µm
pH of 4.6 (so acidic)
contains hydrolytic enzymes and acid Hydrolases
lysosomal membrane is composed of glycosylated proteins that act as a protective lining next to acidic lumen.

170
Q

Function of lysosomes

A

Plays a role in maintaining in regulating sell, homeostasis by degrading intracellular components and providing cell degradation products
1. Autophagy
2. Degradation of internalized material

171
Q

Autophagy

A

a normal disassembly of unnecessary or dysfunctional cellular components organelle turnover.
- Isolation membrane derived from ER engulf target organelles to form auto phagosome.
— Lysosome fuses with ER, derived auto phagocytic vesicle deform auto lysosome.
- Content of auto lysosome is enzymatically digested in released (exocytosis)

172
Q

Degradation of internalized material

A

Recycling of plasma, membrane components like receptors and extracellular material
destroy pathogens, like bacteria and viruses (in phagocytic cells)

173
Q

Phagocytic cell

A

Engulfs bacteria through a process called phagocytosis

174
Q

Phagocytosis

A

The pathogen is degraded by lysosomes that associated with the pathogen, containing vesicle hydrolytic enzymes inside lysosomes, degrade and kill. The pathogen debris is released outside.

175
Q

How do you neutrophils know to attack bacteria?

A

The cell bacteria is produce chemo attractants for which neutrophils white blood cells have receptors this allows the neutrophils to move in the direction of and target bacteria

176
Q

Plant vacuoles

A

Vacuoles are fluid filled membrane bound they can take up to 90% of the cells volume

177
Q

Plant vacuole function broad

A

vacuoles are involved in the regulation of cytoplasmic pH sequestration of toxic ions regulation of cell rigidity storage of amino acids sugars, and CO2 in the form of malate

178
Q

Tonoplast

A

Vacuolar membrane that contains active transport systems that allow ions in molecules to transport looks like a dotted circle

179
Q

Function of vacuoles specific

A
  1. Intracellular digestion (comparable to lysosomes.] slightly low pH of five, acid Hydro laces
  2. Mechanical support turgor pressure gives rigidity to plant supports soft tissues stretches well during growth.
  3. Storage of solutes and macromolecules chemical storage, toxic compounds and pigments like anthocyanin
180
Q

Coatomer for endocytosis

A

Clathrin & AP (adaptor protein) complex
vesicles with these proteins move from trans Golgi Nettwerk to other vesicles, such as lysosomes endosome’s or plant vacuoles
Coated vesicles also help form endocytotic vesicles to move from plasma membrane to endosomes or lysosome

181
Q

Microtubule associated non-motor proteins

A

Control microtubules organization inside a cell
power intracellular transport
Kinesin & dyenin
Use ATP to generate force
can move material along microtubule track
can generate sliding force between microtubules

182
Q

Kinesin

A

+ end directed

183
Q

Dyenin

A
  • end directed
184
Q

Motor proteins, and movement

A
  1. ATP binding to the leading head induces a confirmational change that swirls the training, trailing head, one on the left 180 greets towards the positive end of the microtubules the force generates a step.
  2. The new leading head quickly binds to a tubular subunit and releases it ADP moving its kinesin cargo forward.
  3. In the trailing head, ATP is hydrolyzed to ADP which leads to detachment from microtubule.
  4. ATP binds to leading head to repeat the reaction cycle.
185
Q

MTOC

A

Microtubule organizing centre
Central site of microtubule assembly
Only found in eucaryotic cells
Two important types, basal bodies, and centrosome

186
Q

Basal bodies microtubules

A

Associated with cilia and flagella

187
Q

Centrosome microtubules

A

Associated with spindle formation motor Mabs can generate sliding force between microtubules, which is important during mitosis and chromosome segregation

188
Q

Cytoskeleton

A

Composed of microtubules, microfilaments and intermediate filaments

189
Q

Microtubules

A

Hollow tube formed from tubulin, dimers, alpha tubulin, and beta tubulin
Polar
Similar to microfilaments

190
Q

Microfilaments

A

Double helix of actin monomers
Thinnest polymer of actin proteins

191
Q

Intermediate filaments

A

Strong fibre made of intermediate filament proteins subunits, 10 to 12 nm in diameter
exclusive to multicellular animal cells not polar, so not used in transport composed of keratin’s in the cytoplasm and especially abundant in axons of neurons, composed of lemons in the nucleus

192
Q

Intermediate, filament function

A

provide structural support and mechanical strength table in comparison to microtubules or microfilaments

193
Q

Micro tubule function

A

Cell shape and support cell movement by cilia and flagella cell division, chromosome segregation, vesicle transport, and organelle arrangement

194
Q

Micro filament function

A

Cell shape and support cell movement by crawling cell division, cytokinesis, vesicle transport, muscle contraction

195
Q

Myosin’s

A

Super family of motor proteins associated with microfilaments divided into two broad groups. Conventional myosins and unconventional myosins

196
Q

Conventional myosins

A

Type two primary motors for muscle contraction

197
Q

Unconventional myosin

A

Type one and type 3 to 18
Generate force and contribute to motility of non-muscle cells

198
Q

Directed sell motility

A

Coordinated activity of actin binding proteins, controlled microfilament formation in a Lamela podium and to allow directed cell movement

199
Q

Lamellipodium

A

Actin projection on the leading edge of a cell looks like a mane of a horse

200
Q

Prolific

A

Actin binding protein, that enhances growth of filaments think pro positive

201
Q

Cofilin

A

Actin binding proteins that disassembles actin filaments think coffin stop

202
Q

Capping protein

A

Blocks the exchange of subunit at the positive end

203
Q

Actin

A

Enzyme that binds and slowly hydrolyzes ATP

204
Q

Phalleidin

A

Toxin found in mushrooms lethal after a few days, when injected into bloodstream prevents the deep polarization of actin fibres

205
Q

Three functions of the nucleus

A

1) storage, replication and repair of genetic material
2) expression of genetic material (transcription of mRNA)
3) ribosome biosynthesis

206
Q

Nucleosome

A

10 nm fiber, composed of four histone proteins

207
Q

Chromatin

A

Condensed DNA, which coils, and then coils coils to form chromatids

208
Q

What can damage DNA?

A

UV light exposure replication airs, chemical exposure, cellular metabolism, ionization, radiation, DNA repair, machinery come and fix it

209
Q

Nuclear envelope

A

Nuclear membrane pores, and Lamina
Two parallel phospholipid bilayer’s separated by 10 to 15 nm of space composed of the outer nuclear membrane and the inner nuclear membrane

210
Q

Outter nuclear membrane, ONM

A

Binds ribosomes and is continuous with rough endoplasmic reticulum

211
Q

Inner nuclear membrane

A

Has integral proteins and connects nuclear lamina

212
Q

Importance of nuclear envelope

A

Separates nuclear content from cytoplasm, separates transcription and translation processes. Selective barrier that allows limited movement between nucleus and cytoplasm small molecules and ions can passively diffuse through it, but large proteins and RNA requires active transport.

213
Q

The nuclear lamina

A

Supports the nuclear envelope thin meshwork of filament proteins, called lemons, intermediate filaments found in animal cells only plants have lemonade, but not made of lemon proteins

214
Q

Where and how is nuclear lamina bound?

A

Nuclear lamina is bound to the inner membrane of the nuclear envelope by integral proteins

215
Q

Nuclear lamina function

A

Provides structural support for nuclear envelope
attachment sites for chromatin

216
Q

Nuclear pore

A

Gateways between cytoplasm and nucleus 3000 to 4000 pores per nucleus complex structure that involves arrangement of different types of proteins

217
Q

Where are nuclear pores found?

A

pores are found where inner and outer membrane fuses

218
Q

Nuclear pore complex

A

Composed of nuclear Porins, a large family of proteins, octagonal symmetry, basket, like projects into cytoplasm and nuclear plasm

219
Q

Supra molecular complex

A

Very big from a protein arrangement point of you 315 to 30 times the size of a ribosome

220
Q

How many molecules per minute purport can the nucleus take in?

A

100

221
Q

How small must molecules be to diffuse within the nucleus for

A

40 KDA or less

222
Q

Regulated movement of a larger molecule through nuclear pore how long does it take?

A

Six molecules per minute per pore

223
Q

NLS

A

Nuclear localized signal
Several positively charged amino acids within proteins sequence regulated movement of proteins, requires it

BIOL*1090 (3 decks)

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