chapter 31 protein synthesis Flashcards

1
Q

which error frequency is intolerable

A

10^-2

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2
Q

the error frequency must not exceed 10^-4 to effectively produce large proteins

A

10^-4

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3
Q

where are amino acids attached in tRNAs

A

to 3’ end to 3’ hydroxyl group of an adenosin

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4
Q

why are certain bases unusually methylated in tRNAs

A

so that they don’t form base pairs and to be accessible for other interaction.
The methylations also give a hydrophobic character that can be used when interacting with certain proteins

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5
Q

about ….. of the bases are paired in tRNAs

A

50 %

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6
Q

tRNA which form of helix does it have

A

A form

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7
Q

Components of tRNA

A
5-phosphorylated terminus 
DHU loop (dihydrouracil)
anticodon loop 
extra arm variable loop 
Tpsi C loop (ribothymine pseudouracil-cystosine)
CCA arm
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8
Q

what is I in anticodons

A

purine base inosin

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9
Q

How is inosin formed

A

deamination of adenosine after the synthesis of the primary transcript

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10
Q

what checks if the codon-anticodon duplex is correct in bacteria

A

the 30s subunit with 16s that form hydrogen bonds with the first two correct nucleotides in the anticodon but not with the wrong ones

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11
Q

why must aminoacids be activated

A

because peptide formation between free aminoacids is not thermodynamically favourable

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12
Q

where are ATPs consumed when activating aminoacids

A

the first one is in the formation of ester bond in aminoacyl-tRNA and the other is considered in driving the reaction forward

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13
Q

how do aminacyl-tRNA synthetases correctly remove or accept the correct amino acid?

A

through acylation sites rejecting ones that are larger than the correct one
hydrolytic sites
cleaving ones that are smaller than wanted

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14
Q

Which parts of tRNAs interact extensively with amino-acyl synthetase

A

acceptor stem and anticodon loop

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15
Q

How many classes of synthetases and the differences?

A

1- CCA is helical in II and hair pin in I
2- I 2’ and II 3’
3- bind ATP in different conformations
4- I monomeric and II dimeric

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16
Q

which subunit is mRNA being translated bound to in bacteria ? what about tRNA?

A

30s subunit
in contact with both
30s and 50s

17
Q

the consensus of shine dalgarno sequence in prokaryotes

18
Q

Factors determining the start of protein synthesis

A

pairing of 3’ of 16s to initiation sites

pairing of anticodon to codon

19
Q

initiation codons for bacteria

A

AUG GUG UUG

20
Q

which tRNA initiates protein synthesis in bacteria

A

tRNAf with N-formylmethionine

21
Q

when is N-formylmethionine removed

A

when 10 aminoacids have been synthesized

22
Q

What enzyme formylates methionin

A

transformylase

23
Q

what is the rate limiting step in protein synthesis in bacteria

A

the formation of 70s initiation complex

24
Q

what is the highly conserved site that interacts with EF-TU in subunit 50s is called? function?

A

sarcin ricin loop interacts with EF-Tu complex and causes the hydrolysis of its GTP releasing EF-Tu-GDP

25
what is accomodation in protein synthesis in bacteria
when structural changes happen moving the aminoacyl-tRNA closer to p-site in subunit 50s
26
which factor recognises and interacts with tRNAf
IF2
27
polyribosome /polysome
Multiple ribosomes translating an mRNA simultaneously
28
tRNAs and stop codons?
They don't exist
29
what recognises stop codons
RFs
30
RF1 and RF2 and RF3
RF 1 : UAA UAG RF2 : UAA UGA RF3: removes the other ones when the protein synthesized is released
31
what does RFs interact with and how?
The peptidyl transferase center on the 50s subunit using a highly conserved loop containing GGQ with glutamine being methylated promoting water molecule attacks on the ester linkage between tRNA and the polypeptide chain
32
How is the 70s complex entirely dissociated
through the hydrolysiss of GTP by binding to EF-G and RRF (ribosome release factor)
33
the initiation factor in eukaryotes?
eIFs
34
when are internal ribosome entry sites are used? The function ?
when there are no 5'caps. They faciltate the association of subunit 40s to mRNA
35
the eukaryotic counterparts of elongation factors in eukaryotes EF-G release factors
EF1alpha EF1Betagamme EF1By EF2 eRF1 and eRF3 to accelerate the activity of eRF1
36
antibiotics that inhibit protein synthesis in eukaryotes? | and how do they operate and what do they affect?
ricin a-sarcin and diptheria they all inhibit elongation ricin and a-sarcin covalently modify rRNA and diptheria covalently modify the elongation factor EF2
37
secretory pathway
cotranslation of a protein directed towards the endoplasmic reticulum
38
a ribosome in eukaryotes remain free in ...... unless directed to the .....ER
cytoplasm, ER
39
the components of translocation across endoplasmic reticulum
1- signal sequence 2- signal recognition particle (SRP) 3- SRP receptor (SR) 4- Translocon