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EoM 2 > Protein Synthesis > Flashcards

Protein Synthesis Flashcards

1
Q

Name the three stop codons

A

UAA, UAG, UGA

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2
Q

Mutation which changes sequence to a stop codon

A

nonsense mutation

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3
Q

Mutation which changes sequence but does not result in an amino acid change

A

silent mutation

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4
Q

Mutation which changes sequence and results in a different amino acid

A

missense mutation

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5
Q

Which arm of tRNA recognizes and binds to mRNA

A

Anticodon Arm

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6
Q

Which arm of tRNA is important for recognizing amino acids?

A

D Arm

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7
Q

Which terminus is the amino acid attachment site on tRNA?

A

3’

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8
Q

Which enzyme “charges” tRNA with their appropriate amino acid?

A

aminoacyl tRNA synthases

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9
Q

Most common “Watson Wobble” binding pair between codon and anti-codon?

A

G-U

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10
Q

What nucleotide in the third position of the tRNA anticodon contributes to the presence of a watson wobble effect?

A

Inosine

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11
Q

What precedes the initiation codon in bacterial mRNA?

A

Shine Dalgarno sequence

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12
Q

mRNA with more than one ribosome translating

A

Polysome

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13
Q

Major checkpoint in protein translation?

A

IF2 / eIF2

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14
Q

What is IF2’s importance?

A

IF2 is necessary for bringing together the large and small subunit. Needs the GTP to GDP cleavage for energy.

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15
Q

How is eIF-2 regulated?

A

Phosphorylation/dephosphorylation

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16
Q

What in eukaryotic translation initiation binds the poly-A tail and brings everything together for efficient translation?

A

PABP

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17
Q

Scanning for the start codon is dependent on…

A

ATP

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18
Q

tRNA binding site - A

A

Holds incoming tRNA

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19
Q

tRNA binding site - P

A

carries growing peptide chain

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20
Q

tRNA binding site - E

A

empty tRNA exists

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21
Q

Brings charged tRNA to the ribosome. Bound to GTP

A

eEF-1α

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22
Q

What happens when eEF-1α/GDP is released?

A

tRNA inserted into the A site (irreversible)

23
Q

Which enzyme catalyzes the formation of peptide bonds in elongation?

A

peptidyltransferase

24
Q

Which elongation factor promotes exchange of bound GDP on eEF-1α for GTP?

A

eEF-1βγ

25
Q

What role do the 5’ and 3’ untranslated regions (UTR) play in translation?

A

They can bind regulatory proteins to modulate translation.

26
Q

How is ferritin mRNA translationally regulated?

A

Iron regulatory protein (IRP) binds to the iron response element in 5’ UTR, blocking translation

27
Q

Translation of ferritin mRNA is blocked under what condition?

A

iron is absent

28
Q

What binds to the 3’ UTR of ceruloplasmin (copper-carrying protein) mRNA during inflammation, inhibiting ribosome recruitment.

A

GAIT

29
Q

Proteins can bind to the _____ in order to direct mRNAs to particular cellular locations?

A

3’ UTR

30
Q

Phosphorylation of eIF-2 and e-IF2B does what?

A

Blocks exchange of GDP for GTP. (Inhibits)

31
Q

Antibiotic used to inhibit initiation by binding to and distorting the structure of the 30S ribosomal subunit (prokaryotic)

A

Streptomycin

32
Q

Inhibits elongation by blocking access of the A site through interaction with the 30S ribosome subunit

A

Tetracyclines

33
Q

Binds and inhibits the peptidyltransferase activity of the 50S ribosome, preventing the formation of peptide bonds and blocking elongation

A

Chloramphenicol

34
Q

Inhibit translocation of the ribosome by binding to the 50S subunit, blocking elongation

A

Erythromcin and clindamycin

35
Q

Structural analog of tyrosyl-tRNA. Enters the A site of the ribosome and is incorporated into the peptide causing premature release of the polypeptide (both prokaryotic and eukaryotic)

A

Puromycin

36
Q

Binds and inhibits the peptidyltransferase activity of the 50S ribosome, preventing the formation of peptide bonds and blocking elongation (prokaryotic)

A

Chloramphenicol

37
Q

Cleaves the adenine residue from the 60S subunit (eukaryotic), making it so that eEF-2 can’t bind

A

Ricin

38
Q

Structural analog of tyrosyl-tRNA. Enters the A site of the ribosome and is incorporated into the peptide causing premature release of the polypeptide (both prokaryotic and eukaryotic)

A

Puromycin

39
Q

Naturally occurring fungicide, interfering with the translocation step in protein synthesis, blocking eukaryotic translational elongation

A

Cyclohexamide

40
Q

Cleaves the adenine residue from the 60S subunit (eukaryotic), making it so that eEF-2 can’t bind

A

Ricin

41
Q

Provides favorable conditions for correct folding, prevents aggregation, and prevents misfolding of proteins. Proteins which remain improperly folded after translation are brought here.

A

Chaperonin

42
Q

Three roles for protein cleavage in protein processing

A

1) removal of the initiator methionine at the N-terminus
2) N-terminal signal sequence targets proteins for transport. This can be cleaved
3) cleavage of large precursors forms active enzyme/hormone

43
Q

Cataylzes interconversion between prolyl isomerases

A

Peptyidyl Prolyl Isomerase

44
Q

Three types of lipid attachments during protein processing

A

1) N-myristoylation
2) prenylation
3) palmitoylation

45
Q

Glycosylphosphatidylinositol (GPI) anchors attach proteins to which side of the ER membrane?

A

luminal

46
Q

ER-associated degradation/quality control chaperones

A

Calnexin and calreticulin

47
Q

Excess of unfolded proteins activates a signaling pathway. Leads to expansion of the ER, production of more chaperones, and apoptosis in extreme cases.

A

Unfolded protein response

48
Q

What is the start codon’s amino acid in prokaryotes?

A

Formyl-methionine (methionine in eukaryotes)

49
Q

eIF-2 binds to what subunit in the preinitiation complex?

A

43S preinitiation complex

50
Q

What is the name of the kinase which can inhibit eIF-2

A

PKR

51
Q

eEF-1alpha uses GTP to do what?

A

Bring the tRNA into the A site

52
Q

What ubiquinates and targets shit for proteosome?

A

APC

53
Q

Which side chain residue does ubiquitin add to?

A

Lysine

EoM 2 (12 decks)

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