PHILLIPS CH11 Flashcards

1
Q

anticodon

A

on tRNA

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2
Q

codon

A

on mRNA

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3
Q

aminoacyl-tRNA synthetase

A

attach amino acids to tRNA (require ATP)
recognize both AA and rRNA, one for each AA

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4
Q

2 subunits of ribosomes

A

small subunit deciphers mRNA
large subunit mediates chemical bond formations

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5
Q

rate of protein synthesis

A

15 AAs

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6
Q

translation factors

A

often GTPases, associate with ribosomes and help with translation

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7
Q

4 regions of tRNA structure

A

acceptor stem and 3 stem-loops (D-loop, T-loop, anticodon loop)

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8
Q

D-loop

A

contains dihydrouridine (D)

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9
Q

T-loop

A

contains ribothymidine (T) and pseudouridine

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10
Q

anticodon loop

A

contains a hypermodified purine (H) after the anticodon to prevent this from base-pairing with mRNA codon

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11
Q

acceptor stem

A

5’ and 3’ ends base pair, 3’ CCA tail binds the AA

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12
Q

draw structures of dihydrouridine, pseudouridine, inosine

A

see notes

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13
Q

discovery of triplet code

A

three insertions or three deletions restores function

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14
Q

number of codons

A

61 sense codons (AA)
3 antisense codons (stop/nonsense - end of protein)

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15
Q

wobble pairing

A

non Watson-Crick base pairing
can occur on the third position of codon
(e.g. UUC and UUU can pair with AAG)
each codon does not need own tRNA

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16
Q

isoacceptors

A

different tRNAs that carry the same amino acids

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17
Q

how do aminoacyl-tRNA synthetases recognize tRNAs?

A

by sequence and structural features called identity elements, often found n anticodon loop or acceptor stem

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18
Q

EFTu

A

protect highly-reactive aminoacyl-tRNAs and deliver to ribosome A site

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19
Q

size exclusion

A

keeps non-cognate AAs that are too big out of the aminoacylation site

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20
Q

editing site

A

site on aminoacyl-tRNA synthetase that accomodates similar or smaller non-cognate AAs to prevent errors in aminoacylation
pre- or post- transfer
(essentially gives another site for wrong AAs to go)

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21
Q

process of aminoacyl-tRNA synthetase adding a correct AA

A

via ATP, AA enters aminoacylation site, tRNA attaches to it, AA cannot enter the editing site, remains attached to tRNA

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22
Q

16S rRNA

A

mediates interaction between tRNA and mRNA

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23
Q

23S rRNA

A

found in peptidyl transferase center, interacts with tRNAs

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24
Q

3 binding sites in ribosomes for tRNAs

A

A: aminoacyl site
P: peptidyl site
E: exit site

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25
Q

initiation (translation in bacteria)

A

initiation factors load initiator methionine tRNA into the P site of the small subunit and the large subunit joins

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26
Q

elongation (translation in bacteria)

A

1) elongation factor Tu loads next aminoacyl tRNA into A site of ribosome
2) ribosomal peptidyl transferase catalyzes peptide bond formation
3) elongation factor G (EFG) promotes movement of the mRNA - tRNA complex places next codon into A site

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27
Q

termination (translation in bacteria)

A

class I release factors recognize the stop codon, tRNA releases polypeptide chain, recycling factors promote dissociation of ribosomal subunits from one another

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28
Q

ribosome recycling

A

dissociation of ribosomal subunits and release of tRNA and mRNA

29
Q

polysomes

A

many ribosomes piled up on the same mRNA (elongates simultaneously)
transcription and translation occur simultaneously only in bacteria

30
Q

GTPases

A

catalyze the hydrolysis of GTP to GDP
EFTu, eIF2, EFG

31
Q

EFTu

A

protects and delivers aminoacyl-tRNA to ribosome A site

32
Q

eIF2

A

loads tRNA methionine into P site during initiation

33
Q

EFG

A

promotes directional movement of mRNA-tRNA complex through ribosome
binds in A site

34
Q

GAPs

A

GTPase activating proteins, promote GTP hydrolysis

35
Q

GEFs

A

guanine-nucleotide exchange factors, promote exchange of GDP to GTP

36
Q

initiator tRNA

A

distinct from tRNA(met), structure prevents binding by elongation factors

tRNA(fMet) in bacteria, tRNAi(Met) in eukaryotes

37
Q

polycistronic

A

having several open reading frames, each frame has its own start and stop codon (e.g. bacterial mRNAs)

38
Q

Shine-Dalgarno sequence

A

polypurine tract 6-8 bases upstream of initiator AUG, usually in initiation codons

39
Q

anti-Shine-Dalgarno sequence

A

polypyrimidine region in the 3’ end of the bacterial 16S rRNA, pairs with Shine-Dalgarno sequence

pairing guides initiator AUG mRNA into P site

40
Q

initiation factors that guide tRNA(fMet)

A

IF1, IF2, IF3

41
Q

IF1 and IF3

A

binds the A and E sites (respectively) of the small ribosomal subunit in the absence of mRNA or tRNA(fMet)

direct the initiator tRNA to P side, stops large ribosomal subunit from binding inappropriately

42
Q

monocistronic

A

mRNA only encoding one protein, eukaryotes

43
Q

AUG recognition in eukaryotes

A

scanning mechanism for first AUG
sensitive to sequence context - kozak sequence

44
Q

kozak sequence

A

consensus sequence containing AUG, dictates initiation efficiency

45
Q

eIF4E

A

binds eukaryotic mRNA 5’ cap

46
Q

PABP

A

binds eukaryotic mRNA 3’ poly A tail

47
Q

closed loop complex / elF4 complex

A

eukaryotic mRNA bound by elF4E (on 5’ cap) and PABP (3’ poly A tail) forms the closed loop, functions as quality control to weed out unfinished/damaged mRNAs

48
Q

pre-initiation complex (translation)

A

40S ribosomal subunit bound to initiation factors, primed to scan mRNA
initiator tRNAi(Met) bound to eIF2

49
Q

eIF5

A

stimulates GTP hydrolysis on eIF2

50
Q

initiation (translation in eukaryotes)

A

pre-initiation complex brought to closed loop complex, scans mRNA for AUG

51
Q

eIF4G

A

brings pre-initiation complex to the closed mRNA loop

52
Q

elongation (in bacteria and eukaryotes)

A

decoding, peptide bond formation, translocation, tRNA in E site leaves

53
Q

decoding

A

EFTu loads next charged tRNA into A site

cognate, near-cognate, non-cognate matches
cognate matches bind strongly with ribosome, stimulates conformational change in ribosome and aminoacyl-tRNA is released to A site

54
Q

peptide bond formation

A

catalyzed between the amino acid in the P site and A site

55
Q

translocation

A

mRNA-tRNA through ribosome move the peptidyl-tRNA from A to P site

56
Q

elF4E

A

binds 5’ cap, required to form the closed loop complex

57
Q

hybrid states model

A

in translocation, tRNAs first move independently, then anti-codon end moves (classic > rotated > classic)

58
Q

class I release factors

A

recognize stop codons in termination
RF1: recognizes UAA and UAG
RF2: recognizes UAA and UGA

59
Q

RRF

A

ribosome recycling factor

along with the EFG, acts as a wedge between ribosomal subunits > ribosome disassembly

60
Q

recoding

A

the genetic code is superseded and an mRNA is read differently than expected

61
Q

nonsense suppression

A

stop codons are misread and termination fails to occur

62
Q

peptidyl transferase

A

catalyzes peptide bond formation in growing polypeptide

63
Q

frameshifting

A

the mRNA shifts so the peptide synthesis proceeds in a different reading frame
ribosome moves by a number that is not 3, usually +1 or -1

64
Q

selenocysteine

A

“21st AA,” similar to cysteine but has selenium instead of sulfur, needed in the catalytic site of some enzymes

65
Q

how is selenocysteine loaded?

A

selenocystein-tRNA matches UGA stop codon, specialized loading protein SelB delivers it (can only deliver when there is a specific hairpin element in RNA)

66
Q

pyrrolysine

A

modified lysine, found in methyltransferase genes at catalytic sites

67
Q

how is pyrrolysine loaded?

A

it has its own aminoacyl-tRNA synthetase and tRNA which recognizes UAG stop codon, EFTu helps load

68
Q

programmed frameshifting of RF2 (termination factor)

A

high RF2: recognizes stop codon
low RF2: +1 frameshift so translation continues to produce RF2