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BIO107 - Cell and Molecular Biology > Translation Process > Flashcards

Translation Process Flashcards

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1
Q

Translation process

A
  1. initiation
  2. elongation
  3. termination
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2
Q

formation of a complex where the mRNA, ribosomes, and initiator tRNA form the translation machinery

A

initiation

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3
Q

forms the translation machinery

A
  • mRNA
  • ribosomes
  • initiator tRNA
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4
Q

synthesis of peptide in a 3-step cycle that repeats each time an amino acid is added

A

elongation

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5
Q

cycle in elongation

A

3-step cycle

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6
Q

halting of translation upon encountering a stop codon

A

termination

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7
Q
  • ribosome-binding site in prokaryotes
  • consensus 5’ AGGAGGU 3’
  • 3-10 nucleotides upstream of the initiation codon
  • complementary to a region at the 3’ end of the 16S RNA
A

Shine Dalgarno sequence

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8
Q

consensus of Shine Dalgarno sequence

A

5’ AGGAGGU 3’

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9
Q

location of Shine Dalgarno sequence

A

3-10 nucleotides upstream of initiation codon

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10
Q

Shine Dalgarno sequence is complementary to where

A

3’ end of 16S RNA

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11
Q
  • usually AUG
  • sometimes GUG or UUG
A

start/initiation codons

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12
Q

other start codons in prokaryotes

A
  • GUG
  • UUG
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13
Q

Prokaryotic initiation factors

A
  1. IF-1
  2. IF-2
  3. IF-3
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14
Q

actively promotes dissociation of ribosomal subunits

A

IF-1

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15
Q

IF-1 function

A

promotes dissociation of ribosomal subunits

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16
Q

binds to 30S subunits to prevent re-association with 50S subunit

A

IF-3

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17
Q

IF-3 function

A

binds to 30S subunits to prevent re-association with 50S subunit

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18
Q

is a GTPase that directs the attachment of fmet-tRNA

A

IF-2

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19
Q

IF-2 function

A

GTPase that directs attachment of fmet-tRNA

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20
Q
  • formulated methionine
  • activated tRNA
A

fmet-tRNA

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21
Q

prokaryotic translation: elongation

A
  1. aminoacyl-tRNA binding at A site
  2. peptide bond formation
  3. translocation from A to P site and from P to E site
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22
Q

aminoacylation

A

EF-Tu with GTP

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23
Q

EF-Tu

A

elongation factor-thermo unstable

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24
Q

function of EF-Tu

A

brings aa-tRNA to ribosome during elongation

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25
Q

activates GDP to GTP

A

EF-Ts

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26
Q

enzyme involved in peptide bond formation

A

peptidyl transferase

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27
Q

translocation from A to P and P to E site

A

EF-G w/ GTP or translocase

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28
Q

what happens to GTP during translocation from A to P and P to E

A

cleaved and ribosome moves along mRNA

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29
Q

when any of 3 stop codons is reached

A

termination

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30
Q

creates UAG stop codon

A

amber mutation

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31
Q

where is amber mutation named after

A

Harris Bernstein (Bernstein = amber in German)

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32
Q

amber mutation

A

UAG

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33
Q

creates UAA stop codon

A

ochre mutation

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34
Q

ochre mutation

A

UAA

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35
Q

creates UGA stop codon

A

opal mutation

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36
Q

opal mutation

A

UGA

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37
Q

recognizes stop codons

A

release factor (protein)

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38
Q

different prokaryotic release factor

A
  1. RF-1
  2. RF-2
  3. RF-3
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39
Q

recognizes UAG and UAA

A

RF-1

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40
Q

recognizes UGA and UAA

A

RF-2

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41
Q

assists RF1 or RF2

A

RF-3

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42
Q

what do RFs activate

A

hydrolysis of peptidyl chain from the tRNA

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43
Q

what are released from the ribosome once it reaches stop codon

A

polypeptide chain and tRNA

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44
Q

Prokaryotic translation inhibitors

A
  1. tetracycline
  2. streptomycin
  3. erythromycin
  4. chloramphenicol
  5. puromycin
45
Q

inhibits binding of tRNAs to ribosome

A

tetracycline

46
Q
  • changes shape of 30s and interferes with normal codon-anticodon pairing
  • misreading
A

streptomycin

47
Q

binds 50S and prevents translocation

A

erythromycin

48
Q

binds 50S and inhibits peptidyl transferase activity

A

chloramphenicol

49
Q
  • resembles 3’ end of aa-tRNA
  • premature chain termination
A

puromycin

50
Q

prokaryotic:
binding to ribosome subunits

A
  • IF1
  • IF3
51
Q

eukaryotic:
binding to ribosome subunits

A
  • eIF3
  • eIF4C
  • eIF6
52
Q

prokaryotic:
- binding to mRNA
- initiator tRNA delivery
- displacement of other factors

A

IF2

53
Q

eukaryotic:
- binding to mRNA

A
  • eIF4B
  • eIF4F
54
Q

eukaryotic:
- initiator tRNA delivery

A
  • eIF2
  • eIF2B
55
Q

eukaryotic:
- displacement of other factors

A

eIF5

56
Q

difference between prokaryote and eukaryote initiation based on where ribosome is located

A

pro: directly on start codon
eu: indirectly locate start codon

57
Q

facilitates prokaryotic initiation

A

Shine-Dalgarno sequence

58
Q

absent in eukaryotes (initiation)

A

RBS (ribosome binding site)

59
Q

what mechanism is involved in eukaryotic initiation

A

scanning mechanism starting at 5’ cap

60
Q
  • formation of pre-initiation complex
  • pre-initiation complex binds to 5’ cap
  • pre-init complex scans mRNA until it locates AUG
  • start codon is usually contained in Kozak consensus
  • once pre-init complex is properly positioned, 60S binds to form 80S initiation complex
A

The Scanning Model

61
Q

pre-initiation complex

A

40S + met-tRNA + eIF2 + GTP

62
Q

assists the binding of pre-init complex to 5’cap

A
  • eIF3 and
  • cap binding complex
63
Q

cap binding complex

A

eIF4F

64
Q

eIF4F

A

eIF4A + eIF4E + eIF4G

65
Q

where is the start codon usually contained in

A

Kozak consensus

66
Q

Kozak consensus

A

5’ ACCAUGG 3’

67
Q

The Scanning Model

A
  1. formation of pre-initiation complex
  2. pre-initiation complex binds to 5’ cap
  3. pre-init complex scans mRNA until it locates AUG. Start codon is usually contained in Kozak consensus
  4. once pre-init complex is properly positioned, 60S binds to form 80S initiation complex
68
Q

binds to form the 80S initiation complex

A

60S

69
Q

what happens after 60S binds and forms 80S

A
  • GTP hydrolysis
  • release of eIFs
70
Q

eukaryotic translation:
elongation

A
  1. eEF-1α
  2. eEF-1βγ
  3. eEF-2
  4. no E site in ribosome
71
Q

eEF-1α : __ (prokaryotes)

A

EF-Tu

72
Q

eEF-1βγ : __ (prokaryotes)

A

EF-Ts

73
Q

eEF-2 : __ (prokaryotes)

A

EF-G

74
Q

eukaryote:
- recognizes all 3 stop codons
- requires ATP

A

eRF1

75
Q

function of eRF1

A

recognizes all 3 stop codons

76
Q
  • stimulates release of eRF1 from the ribosome after termination
  • assists eRF1
A

eRF2

77
Q

function of eRF2

A

stimulates release of eRF1 from ribosome after termination

78
Q

Accuracy of Protein Synthesis

A
  1. charging tRNA with correct aa
  2. codon-anticodon
  3. specific contacts between tRNA, mRNA, and rRNA within A site
  4. proof-reading by rejecting an incorrect aminoacyl-tRNA before it can donate its aa
79
Q

what is involved in protein targeting in eukaryotes

A
  1. signal peptide
  2. signal recognition particle (SRP)
80
Q

found in the N-terminal of the nascent protein

A

signal peptide

81
Q

immediate product of translation that is inactive

A

nascent protein

82
Q

recognizes signal peptide

A

signal recognition particle (SRP)

83
Q

what does the SRP do

A
  • recognize signal peptide
  • binds to ribosome to arrest translation
84
Q

where does the SRP with arrested ribosome binds to

A

SRP receptor

85
Q

where is the SRP receptor found

A

Cytosolic face of rough ER membrane

86
Q

where the ribosome attaches to trigger the release of SRP

A

ribosome receptor protein

87
Q

what happens when ribosome attaches to ribosome receptor protein

A

release of SRP for re-use

88
Q

once, SRP is released, what happens to the ribosome

A

continues translation and nascent protein is pushed through rough ER’s lumen

89
Q

what happens as the nascent protein passes through the rough ER’s lumen

A

signal peptidase cleaves off signal peptide

90
Q

what happens to the protein inside the rough ER’s lumen

A

glycosylated

91
Q

control the final location of the protein

A

pattern of glycosylation

92
Q

Events in Protein Targeting

A
  1. SRP recognizes singal peptide, binds to ribosome to arrest translation
  2. SRP with arrested ribosome binds to SRP receptor on cytosolic face of rough ER
  3. ribosome attaches to ribosome receptor protein, triggers release of SRP
  4. ribosome continues translation, nascent protein pushed through rough ER’s lumen
  5. as nascent passes through, signal peptidase cleaves off signal peptide
  6. protein is glycosylated to control its final location
93
Q

Some Post-Translational Modifications

A
  1. glycosylation
  2. hydroxylation
  3. acetylation
  4. phophorylation
94
Q

addition of -OH group like in the formation of 4-hydroxyproline in collagen

A

hydroxylation

95
Q

addition of -COCH3 group such as in histone proteins

A

acetylation

96
Q

addition of -PO43- group in tyrosine, serine, and threonine residues

A

phosphorylation

97
Q
  • reversible
  • activation/inactivation of enzyme activity
  • modulation of molecular interactions
  • signaling
A

phosphorylation

98
Q
  • protein stability
  • protection of N terminus
  • regulation of protein-DNA interactions (histones)
A

acetylation

99
Q

regulation of gene expression

A

methylation

100
Q
  • cellular localizatio and targeting signals
  • membrane tethering
  • mediator of protein-protein interactions
A

acylation, fatty acid modification

101
Q
  • excreted proteins
  • cell-cell recognition/signaling O-GlcNAc
  • reversible
  • regulatory functions
A

glycosylation (N-linked, O-linked)

102
Q

protein stability and protein-ligand interactions

A

hydroxyproline

103
Q

modulator of protein-protein and receptor-ligand interactions

A

sulfation (sTyr)

104
Q
  • intra- and intermolecular crosslink
  • protein stability
A

disulfide bond formation

105
Q
  • possible regulator of protein-ligand and protein-protein interactions
  • common chemical artifact
A

deamidation

106
Q
  • protein stability
  • blocked N terminus
A

pyroglutamic acid

107
Q
  • destruction signal
  • after tryptic digestion
  • site is modifed with Gly-Gly dipeptide
A

ubiquitination

108
Q

oxidative damage during inflammation

A

nitration of tyrosine

BIO107 - Cell and Molecular Biology (18 decks)

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