BIOL 1090 FINAL Flashcards

1
Q

What do cells require?

A

Differentiation, information, chemistry, compartments.

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2
Q

What are the characteristics of prokaryotes?

A

No nuclei, no organelles, no DNA, can’t synthesize RNA, can’t divide, limited repair abilities.

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3
Q

Why is RBC dying off beneficial?

A

Allows to accommodate max hemoglobin carrying capacity.

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4
Q

What is the method by which RBC eject their nucleus?

A

Enucleation.

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5
Q

What is differentiation?

A

The process by which cells become specialized.

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6
Q

What experiment tested the chemical origin of life?

A

Miller-Urey (1952).

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7
Q

What is abiogenesis?

A

Chemical origin of life establishes physical boundary.

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8
Q

Who discovered cells?

A

Robert Hooke in 1665.

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9
Q

What are the elements of cell theory?

A
  • All cells come from other cells
  • Cells are the basic unit of life
  • All living things are made of cells
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10
Q

What are the properties of cells?

A

Highly complex and organized, controlled by genetic program, can reproduce, make and use energy, carry out chemical reactions, engage in mechanical activities, respond to stimuli, self-regulate, evolve.

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11
Q

What is the genetic material of prokaryotes found in?

A

Nucleoid.

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12
Q

How is genetic material in eukaryotes organized?

A

Into chromosomes.

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13
Q

What are the additional structures found in plant cells?

A

Cell walls, vacuoles, chloroplasts, plasmodesmata.

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14
Q

What structures are found in animal cells?

A

Lysosomes and microvilli.

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15
Q

What type of organism is a slime mold?

A

Single celled, sexual reproduction, multinucleated.

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16
Q

What are viruses unable to do?

A

Can’t reproduce outside of living cells.

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17
Q

What is a viron?

A

An inanimate particle outside of a cell.

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18
Q

What is a capsid?

A

Protein capsule of a virus.

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19
Q

How are viruses categorized?

A

Based on type of genome and method of replication.

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20
Q

What is the Baltimore classification?

A

A system that categorizes viruses based on their genome and replication method.

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21
Q

What is an example of a retrovirus?

A

HIV.

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22
Q

What virus affects the liver?

A

Hepatitis B (Hep B).

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23
Q

What virus causes hemorrhagic fever?

A

Ebola.

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24
Q

What type of illnesses does Adenovirus cause?

A

Respiratory illness, eye infections.

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25
Q

How many viruses have been described?

A

5000.

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26
Q

What is CRISPR-Cas?

A

An immune-like system that plays a role in anti-viral defense.

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27
Q

What is lytic viral replication?

A

Production of virus ruptures and kills the cell.

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28
Q

What is non-lytic viral replication?

A

Viral DNA inserted, cells can survive but have impaired function.

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29
Q

What is a monopartite genome?

A

The entire genome is contained in a single nucleic acid segment.

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30
Q

What is a multipartite genome?

A

Genome occupies several nucleic acid segments.

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31
Q

How many types of rabies are known?

A

7.

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32
Q

How is Zika virus transmitted?

A

Mosquitoes, bodily fluids, sexual contact.

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33
Q

What is microcephaly?

A

Abnormally small head.

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34
Q

What are the effects of microcephaly?

A

Motor and speech delays, intellectual disability, seizures, balance problems.

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35
Q

When does neurogenesis occur?

A

Week 10-25.

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36
Q

When does gliogenesis occur?

A

Week 25-40.

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37
Q

How do RNA vaccines work?

A

Trick the body into producing antigen.

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38
Q

How does replicase work in RNA vaccines?

A

Makes lots of copies of the RNA template.

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39
Q

What are the functions of biological membranes?

A

Define cell boundary, define compartments, control movement in/out, allow response to stimuli, enable interactions, provide scaffolding.

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40
Q

What is the plasma membrane?

A

A trilaminar membrane.

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41
Q

How thick is the plasma membrane?

A

6nm.

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42
Q

What is the lipid bilayer made of?

A

Phospholipids.

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43
Q

What are micelles?

A

Structures with 1 head and 1 tail.

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44
Q

What are liposomes?

A

Structures with 2 heads and 2 tails.

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45
Q

What are sphingolipids important for?

A

Signal transduction and cell recognition.

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46
Q

Where does the synthesis of phospholipids occur?

A

At the interface of cytosol and outer ER membrane.

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47
Q

What is the process of phospholipid synthesis?

A

FA activated by CoA, inserted into cytosolic leaflet, phosphate removed by phosphatase, choline linked to P via choline phosphotransferase.

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48
Q

What do flippase and floppase do?

A

Transfer phospholipids to other leaflet.

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49
Q

What are proteins embedded in the phospholipid bilayer?

A

They perform various functions.

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50
Q

What are myelin sheaths?

A

Layers of PM wrapped around neuron’s axon, increasing speed of electrical impulses.

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51
Q

What is the IMM?

A

Very high concentration of protein needed for ETC and ATP synthesis.

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52
Q

What are the three classes of membrane proteins?

A

Integral, peripheral, lipid-anchored.

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53
Q

What is the function of integral proteins?

A

Transport nutrients and ions, communication, attachment.

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54
Q

What is the symmetry of leaflets in the plasma membrane?

A

Asymmetrical.

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55
Q

How does increased temperature affect the lipid bilayer?

A

Increases fluidity, known as liquid crystal.

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56
Q

How does decreased temperature affect the lipid bilayer?

A

Decreases fluidity, known as crystalline gel.

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57
Q

What is the effect of unsaturated lipids on fluidity?

A

Increase fluidity.

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58
Q

What is the effect of saturated lipids on fluidity?

A

Decrease fluidity.

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59
Q

What does a balanced membrane allow for?

A

Mechanical support and flexibility, membrane assembly and modification, dynamic interactions.

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60
Q

What is the function of cholesterol in membranes?

A

Modulates membrane fluidity.

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61
Q

What is a bidirectional regulator of membrane fluidity?

A

Cholesterol.

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62
Q

What is the transmembrane protein domain?

A

Peptide sequence, hydrophobic, spans across the PM.

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63
Q

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

A

Alpha helix.

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64
Q

What are tetraspanins?

A

A superfamily of membrane proteins found in all multicellular eukaryotes.

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65
Q

What is the function of tetraspanins?

A

Cell adhesion, motility, and proliferation.

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66
Q

What is simple diffusion?

A

Nonmediated transport for small, uncharged molecules.

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67
Q

What is diffusion through a channel?

A

Nonmediated transport for small, charged molecules.

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68
Q

What is facilitated diffusion?

A

Mediated, passive transport.

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69
Q

What is active transport?

A

Mediated, active transport.

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70
Q

What is gated ion channels?

A

Transport that can be turned on/off in response to signals.

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71
Q

What is action potential?

A

Passage of electric signal down a nerve.

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72
Q

What is a ligand-gated channel?

A

Responds to binding of a molecule on its surface, causing a conformational change.

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73
Q

What is tetrodotoxin?

A

Discovered in pufferfish, Na+ channel blocker, causes death by respiratory failure.

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74
Q

What is curare?

A

Found in plants, occupies the same position on receptor as Ach, causing muscles not to move.

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75
Q

What is a symporter?

A

Moving from lower to higher concentration, must rely on the chemical gradient of another molecule.

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76
Q

What happens to a cell in a hypertonic solution?

A

Cell shrivels.

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77
Q

What happens to a cell in a hypotonic solution?

A

Cell bursts.

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78
Q

What does signal transduction allow cells to do?

A

Grow, divide, survive, move, differentiate, regulate metabolic activity.

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79
Q

What is a ligand?

A

A small molecule that binds to a receptor, changing its conformation.

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80
Q

What are the three stages of signal transduction?

A

Binding of ligand to receptor, signal transduction, cellular response.

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81
Q

What diseases are caused by defects in signal transduction?

A

Cancer, diabetes, brain disorders.

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82
Q

What is glycogenolysis?

A

The process of converting glycogen to glucose, often stimulated by epinephrine.

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83
Q

What is glycogenin?

A

An enzyme that acts as a primer to polymerize glucose molecules in a state of low blood sugar.

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84
Q

What is an example of a community of cells?

A

Skin.

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85
Q

What are the functions of the extracellular matrix?

A

Cell adherence, communication, cell shape, filter.

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86
Q

What are plant cell walls composed of?

A

Cellulose, hemicellulose, pectin, and proteins.

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87
Q

What is the function of the cell wall?

A

To protect and support the cell.

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88
Q

What is symbiosis?

A

Living together.

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89
Q

What is aerobic respiration?

A

Converting energy in food to ATP in the presence of oxygen.

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90
Q

What is photosynthesis?

A

Converting carbon dioxide to oxygen and carbohydrates.

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91
Q

What is the double membrane organelle?

A

Mitochondria.

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92
Q

What are the characteristics of the outer mitochondrial membrane (OMM)?

A

Contains many enzymes and large porins.

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93
Q

What are cristae?

A

Double layer folds in the inner mitochondrial membrane (IMM).

94
Q

What is the IMM rich in?

A

Cardiolipin.

95
Q

What is the matrix of mitochondria?

A

High protein content, gel consistency, many ribosomes.

96
Q

What are the four compartments of mitochondria?

A

OMM, IMM, intermembrane space, matrix.

97
Q

What is substrate-level phosphorylation?

A

The formation of ATP by directly transferring a phosphate group to ADP from an intermediate substrate in catabolism.

98
Q

What is oxidative phosphorylation?

A

The production of ATP using energy derived from the redox reactions of an electron transport chain; the third major stage of cellular respiration.

99
Q

What happens during oxidation?

A

Lose electrons.

100
Q

What happens during reduction?

A

Gain electrons.

101
Q

Where do light-dependent reactions occur?

A

In the thylakoid membrane.

102
Q

Where do light-independent reactions occur?

A

In the stroma.

103
Q

What is apoptosis?

A

Programmed cell death.

104
Q

What characterizes apoptosis?

A

Shrinkage of cell, blebbing, fragmentation of DNA, loss of attachment to other cells, engulfment by phagocytosis.

105
Q

What is the intrinsic pathway of apoptosis?

A

Causes change in mitochondria to leak Cytochrome C, committing the cell to apoptosis.

106
Q

What happens with too little apoptosis?

A

Cancer.

107
Q

What happens with too much apoptosis?

A

Alzheimer’s, Huntington’s, Parkinson’s.

108
Q

What is GFP (green fluorescent protein)?

A

Used in live imaging by ‘tagging’ a protein with a fluorescent molecule.

109
Q

What is vesicular transport?

A

Transport of large particles and macromolecules across plasma membranes.

110
Q

What are the types of vesicle trafficking?

A

Movement of vesicle, tethering to target compartment, docking to target compartment, fusion of vesicle and target membrane.

111
Q

What are membrane-bound organelles found in the cell?

A

ER, vesicles, Golgi complex, lysosomes, vacuoles.

112
Q

Where is mucin secreted?

A

Rough ER.

113
Q

What is the function of the rough ER?

A

Synthesis of many proteins and glycosylation of proteins.

114
Q

What is the function of the smooth ER?

A

Primary site of lipid synthesis and detoxification.

115
Q

Why is Ca2+ excluded from cytosol?

A

Does not bind water well, it will precipitate phosphates and make proteins insoluble.

116
Q

How do ribosomes synthesize polypeptides from mRNA?

A

Initiation factor recruits MET, scans mRNA from AUG codon.

117
Q

Where does RER and protein translation begin?

A

On free ribosome.

118
Q

What are the two options for translation completion?

A

By free ribosomes or ER bound ribosomes.

119
Q

For translation completed on free ribosomes, what proteins are produced?

A

Cystolic proteins, peripheral membrane proteins, proteins targeted to nucleus, mitochondria, peroxisomes, and chloroplasts.

120
Q

For translation completed on ER bound ribosomes, what proteins are produced?

A

Secreted proteins, integral membrane proteins, soluble proteins associated with the lumen of the endomembrane system.

121
Q

What directs synthesis to the ER?

A

Signal sequence located in the amino terminus, containing hydrophobic AA.

122
Q

What is the function of SRP?

A

Binds to signal sequence, stops translation process, targets the whole translation complex to ER.

123
Q

What happens once the SRP is released?

A

Ribosome binds to translocon and protein synthesis resumes.

124
Q

What is cotranslational protein import?

A

The process where proteins are imported into the ER during translation.

125
Q

What is the TOM complex equivalent to?

A

SRO complex.

126
Q

What options do proteins targeted to the lumen have?

A

Be retained in the ER lumen or transported from ER to Golgi for further modification.

127
Q

What is a microbody?

A

Peroxisome.

128
Q

What is the function of peroxisomes?

A

Catabolizes long chain FA, reduces reactive oxygen species, biosynthesis of plasmalogens.

129
Q

What is the function of catalase?

A

Breaks down hydrogen peroxide into water and oxygen.

130
Q

What syndrome is associated with brain development defects?

A

Zellweger syndrome.

131
Q

How is Zellweger syndrome inherited?

A

Autosomal recessive.

132
Q

What mutation causes cystic fibrosis?

A

Mutation in CFTR.

133
Q

What does CFTR stand for?

A

Cystic fibrosis transmembrane conductance regulator.

134
Q

What mutation accounts for 2/3 of CF cases worldwide?

A

Deletion of 3 nucleotides, resulting in loss of AA phenylalanine.

135
Q

What do CFTR modulators do?

A

Allow soluble proteins to enter the endomembrane system.

136
Q

Where are proteins targeted to mitochondria and chloroplasts synthesized?

A

Completely in the cytoplasm.

137
Q

In what direction does material move from the ER to Golgi to PM?

A

Proximal to distal.

138
Q

What is the order of material movement through the Golgi?

A

CGN to MG to TGN.

139
Q

What is the structure of the Golgi complex?

A

Smooth, flat, cisternae; ~8 stacked, curved; shows polarity, biochemically unique, membrane supported by protein skeleton.

140
Q

What is the function of the Golgi?

A

Sorting station: determines whether proteins continue to Golgi or are shipped back.

141
Q

What does the CGN do?

A

Sorts proteins into different types of vesicles.

142
Q

What is the processing plant of the cell?

A

Golgi.

143
Q

What are the two functions of coat proteins?

A

Help for vesicle formation & help select cargo that will go in vesicle.

144
Q

What does COP stand for?

A

Coat protein complex.

145
Q

In what direction do COPI and COPII move?

A

COPI moves in retrograde direction, COPII moves in anterograde direction.

146
Q

What are COPI and COPII?

A

Protein complexes that assemble on the cytosolic surface at the site where budding occurs.

147
Q

What is an example of a regulated secretory pathway?

A

Insulin and neurotransmitter secretion.

148
Q

What is an example of a constitutive secretory pathway?

A

Mucin secretion.

149
Q

What are lysosomes?

A

Digestive organelles with low internal pH and enzymes.

150
Q

What is the lysosome membrane composed of?

A

Glycosylated proteins, acting as a protective lining next to the acidic lumen.

151
Q

Where do AP/Clathrin-coated vesicles move from?

A

From TGN to other vesicles (lysosomes, endosomes, plant vacuoles).

152
Q

How are macromolecules delivered to lysosomes?

A

Via vesicles.

153
Q

What is autophagy?

A

Normal disassembly of unnecessary/dysfunctional cellular components.

154
Q

What is an autophagic vesicle called?

A

Autophagosome.

155
Q

What forms when a lysosome fuses with an ER-derived autophagic vesicle?

A

Autolysosome.

156
Q

What is the process of decomposition of intracellular components via lysosomes?

A

Autophagy.

157
Q

What is autophagy dysfunction associated with?

A

Neurodegenerative diseases, tumorigenesis, etc.

158
Q

What do hydrolytic enzymes inside lysosomes do?

A

Degrade and kill pathogens.

159
Q

What is a plant vacuole?

A

Fluid-filled, membrane-bound, can take up to 90% of cell’s volume.

160
Q

What is the function of plant vacuoles?

A

Regulate pH, sequestration of toxic ions, cell turgor regulation, storage of AA, sugars, and carbon dioxide.

161
Q

What is the tonoplast?

A

The vacuolar membrane, containing active transport systems that allow ion and molecule transport.

162
Q

What is turgor pressure?

A

Gives rigidity and stretches the cell wall during growth.

163
Q

What are the functions of the cytoskeleton?

A

Structural support, spatial organization within the cell, intracellular transport, contractility, and motility.

164
Q

What are the three components of the cytoskeleton?

A

Microfilaments, microtubules, intermediate filaments.

165
Q

What is the largest cytoskeletal element?

A

Microtubules.

166
Q

What are the two proteins in microtubules?

A

Alpha and beta.

167
Q

What are the two major types of microtubules?

A

Axonemal MT and cytoplasmic MT.

168
Q

What are the properties of axonemal microtubules?

A

Highly organized, stable, involved in cell movement.

169
Q

What are the properties of cytoplasmic microtubules?

A

Loosely organized, dynamic, located in cytosol.

170
Q

What is the structure of microtubules?

A

Heterodimers form protofilaments, 13 form a hollow cylinder.

171
Q

What is the fast-growing end of microtubules?

A

+ end.

172
Q

What is the slow-growing end of microtubules?

A
  • end.
173
Q

What is structural polarity important for?

A

MT growth and direction of movement of material along MT.

174
Q

What is dynamic instability?

A

Rapid turnover of most MTs; shrinkage occurs rapidly at the + end.

175
Q

What is the central site of microtubule assembly?

A

Microtubule-organizing center (MTOC).

176
Q

What do MAPs do?

A

Modulate assembly, mediate interactions with other cellular structures.

177
Q

What are the classes of MAPs?

A

Non-motor MAP and motor MAP.

178
Q

What is the function of non-motor MAPs?

A

Control MT organization in cytosol.

179
Q

What does defective Tau protein lead to?

A

Alzheimer’s.

180
Q

What is the function of motor MAPs?

A

Moves material along MT using ATP, generates sliding force.

181
Q

What are the two types of motor MAPs?

A

Kinesin and dynein.

182
Q

What direction is kinesin directed?

A

+ end directed, dynamic.

183
Q

What direction is dynein directed?

A
  • end directed, stable.
184
Q

What is the force generating step?

A

ATP binds to leading head, causing a conformation change, and the trailing head swings.

185
Q

What are the two most important MTOCs?

A

Basal bodies (cilia and flagella) and centrosome (spindle formation).

186
Q

Where are intermediate filaments found?

A

Only in multicellular animal cells.

187
Q

What is the function of intermediate filaments?

A

Support and strength.

188
Q

How do intermediate filaments compare to microtubules and microfilaments?

A

They are more stable.

189
Q

What are microfilaments (MF) functions?

A

Cell shape, cell movement, vesicle transport, muscle contraction, cytokinesis.

190
Q

What is microfilament polymer made of?

A

Actin.

191
Q

What is the structure of microfilaments?

A

A double helix of actin monomers.

192
Q

What are the properties of microfilaments?

A

Polar, have + (assembles quickly) and - (assembles slowly) ends.

193
Q

What are early nucleation of G-actin polymerization?

A

Slow.

194
Q

How can microfilaments be arranged?

A

Loosely or tightly.

195
Q

What organizes the structure of microfilaments?

A

Actin-binding proteins.

196
Q

What does profilin do?

A

Enhances growth of filaments.

197
Q

What does cofilin do?

A

Disassembles actin filaments.

198
Q

What does capping protein do?

A

Blocks exchange of subunit at + end.

199
Q

What is myosin?

A

A superfamily of motor proteins associated with microfilaments.

200
Q

What are the two groups of myosin?

A

Conventional and unconventional.

201
Q

What is the function of conventional myosin?

A

Muscle contraction.

202
Q

What is the function of unconventional myosin?

A

Generate force, contribute to motility in non-muscle cells.

203
Q

What is the function of the nucleus?

A

Storage, replication, repair, expression of genetic material, ribosome biosynthesis.

204
Q

What are the six levels of genetic material organization?

A

DNA duplex, nucleosome fiber, chromatin fiber, coiled chromatin fiber, coiled coil, condensed chromatid.

205
Q

What can damage DNA?

A

UV, chemical exposure, cellular metabolism, replication errors, ionizing radiation.

206
Q

What is the function of RNA polymerase?

A

Reads DNA sequence and produces complementary antiparallel strand of RNA.

207
Q

Where do ribosomes translate mRNA?

A

In the cytosol.

208
Q

What are introns and exons?

A

Introns are excised, exons are spliced.

209
Q

What does mRNA receive before leaving the nucleus?

A

5’ cap and poly A tail.

210
Q

What are the 6 levels of genetic material organization?

A

DNA duplex, nucleosome fiber, chromatin fiber, coiled chromatin fiber, coiled coil, condensed chromatid.

211
Q

What can damage DNA?

A

UV, chemical exposure, cellular metabolism, replication errors, ionization radiation.

212
Q

What is the function of RNA polymerase?

A

Read DNA sequence and produce complementary antiparallel strand of RNA.

213
Q

Where do ribosomes translate mRNA?

A

Cytosol.

214
Q

What modifications does mRNA receive before leaving the nucleus?

A

5’ cap, poly A tail.

215
Q

What are the 3 parts of the nuclear envelope?

A

Nuclear membrane, nuclear pores, nuclear lamina.

216
Q

What are the 3 parts of nuclear content?

A

Chromatin, nucleoplasm, nucleolus.

217
Q

What binds ribosomes and is continuous with the RER?

A

Outer nuclear membrane (ONM).

218
Q

What connects integral proteins to the nuclear lamina?

A

Inner nuclear membrane (INM).

219
Q

What is the importance of the nuclear envelope?

A

Separates content from cytoplasm, separates transcription/translation processes, selective barrier.

220
Q

What is the nuclear lamina?

A

A thin meshwork of filamentous proteins.

221
Q

How is the lamina bound to the inner membrane of the nuclear envelope?

A

By integral membrane proteins.

222
Q

What provides structural support for the nuclear envelope?

A

Nuclear lamina.

223
Q

What is the gateway between cytoplasm and nucleus?

A

Nuclear pore.

224
Q

Where are nuclear pores found?

A

Where inner and outer membrane fuse.

225
Q

What are nucleoporins?

A

Octagonal, supramolecular, 15-30x size of ribosome.

226
Q

What is passive diffusion?

A

40kDA or less, rapid, 100mol/min/pore.

227
Q

What is regulated movement?

A

Larger molecules, slower, 6mol/min/pore.

228
Q

What is required for the regulated movement of proteins into the nucleus?

A

Nuclear localization signal (NLS).

229
Q

What is importin?

A

Transport receptor that binds to the NLS of the cargo and interacts with the nuclear pore.

230
Q

Why is nuclear import/export important?

A

For nucleotides for transcription, structural & DNA packaging proteins, proteins for DNA replication, repair, transcription, proteins for RNA processing/export, proteins for ribosome synthesis/export.

231
Q

What is the largest structure inside the nucleus?

A

Nucleolus.

232
Q

What is the primary function of the nucleolus?

A

Biosynthesis of ribosomes.