Exam 4 Protein Metabolism Flashcards

1
Q

What is the first amino acid in eukaryotic translation initiation?

A

Methionine (Met), carried by initiator tRNA (tRNAi).

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2
Q

How does prokaryotic translation initiation differ?

A

UsesN-formylmethionine (fMet)instead of regular methionine.

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3
Q

What is the wobble hypothesis?

A

Nontraditional base-pairing between the 5′ nucleotide (1st nucleotide) of the anticodon and the 3′-nucleotide (last nucleotide) of the codon.

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4
Q

How does wobble pairing reduce the number of tRNAs needed?

A

One tRNA can recognize multiple codons (e.g., inosine (I) in tRNA pairs with U, C, or A).

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5
Q

What are the ribosomal subunits in prokaryotes?

A

30S (small)+50S (large)=70S ribosome.

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6
Q

What are the ribosomal subunits in eukaryotes?

A

40S (small)+60S (large)=80S ribosome.

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7
Q

Name the three tRNA binding sites on ribosomes.

A

A site(aminoacyl),P site(peptidyl),E site(exit).

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8
Q

What modified bases are found in tRNA (besides A, C, G, U)?

A

Inosine (I), pseudouridine (Ψ), dihydrouridine (D), methylated bases (e.g., m⁷G).

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9
Q

If the codon isUUC, what is the anticodon?

A

AAG(orGAAif wobble pairing allows inosine at the 5′ end).

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10
Q

What enzyme attaches amino acids to tRNA? Is it specific?

A

Aminoacyl-tRNA synthetase(specific to each amino acid and tRNA).

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11
Q

What bond links amino acids to tRNA?

A

Ester bondbetween the amino acid’s carboxyl group and tRNA’s 3′-OH.

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12
Q

What are the two steps of tRNA “charging”?

A
  1. Amino acid + ATP → aminoacyl-AMP + PPi. 2. Aminoacyl-AMP + tRNA → aminoacyl-tRNA + AMP.
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13
Q

In eukaryotes, all proteins start with which amino acid?

A

Methionine (Met)at theN-terminus.

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14
Q

What is required for bacterial initiation complex formation?

A

mRNA, fMet-tRNA, 30S/50S subunits, initiation factors (IF-1, IF-2, IF-3), GTP.

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15
Q

What delivers aminoacyl-tRNA to the ribosome during elongation? Elongation factors?

A

EF-G (bacteria) or eEF-2 (eukaryotes); EF-Tu-GTP(bacteria) /eEF1α-GTP(eukaryotes).

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16
Q

What is a polysome?

A

Multiple ribosomes translating the same mRNA simultaneously.

17
Q

How many NTPs are hydrolyzed per amino acid added?

A

4(2 ATP for tRNA charging + 2 GTP for elongation/translocation).

18
Q

Translate this mRNA:5′-AUGUUUCAAUAA-3′.

A

Met-Phe-Gln-Stop(AUG = Met, UUU = Phe, CAA = Gln, UAA = Stop).

19
Q

What happens if the mRNA lacks a stop codon?

A

Ribosome stalls;NSD (non stop decay)rescues by tagging the protein for degradation.

20
Q

What are the ribosome binding sites for tRNA during elongation?

A

A site(incoming tRNA),P site(growing peptide),E site(exiting tRNA).

21
Q

True or False: Ribosome assembly on mRNA requires ATP.

A

False(uses GTP for initiation/elongation).

22
Q

True or False: tRNA charging requires aminoacyl-AMP formation.

A

True(intermediate step before tRNA attachment).

23
Q

What drives translocation of the ribosome?

A

EF-G-GTPhydrolysis (bacteria) /eEF2-GTP(eukaryotes).

24
Q

True or False: Translation termination requires GTP hydrolysis.

A

False(uses release factors, but no NTP).

25
Order these steps: Peptide bond formation, tRNA release, 50S binding, aminoacyl-tRNA binding.
1. 50S binds 30S initiation complex. 2. Aminoacyl-tRNA binds A site. 3. Peptide bond forms. 4. tRNA released.
26
What NTP is hydrolyzed during peptide translocation?
GTP (by EF-G/eEF2).
27
True or False: Eukaryotic initiation involves 5′-3′ mRNA looping.
True (5′ cap and 3′ poly-A tail interact via initiation factors).
28
True or False: Prokaryotes use Met (not fMet) for initiation.
False (prokaryotes use fMet; eukaryotes use Met).
29
True or False: Prokaryotic transcription/translation are coupled.
True (no nucleus allows simultaneous processes).
30
What are the three steps of bacterial elongation?
Aminoacyl-tRNA binding: EF-Tu-GTP delivers correct charged tRNA to A site, matching the mRNA codon. Peptide bond formation: Peptidyl transferase (23S rRNA in 50S subunit) catalyzes bond formation b/w P-site peptide & A-site amino acid. Translocation: EF-G-GTP hydrolyzes GTP to shift ribosome, moving the tRNA-peptide to P site & ejecting the deacylated tRNA from the E site.
31
Name four posttranslational modifications.
Proteolytic cleavage,  phosphorylation,  glycosylation,  ubiquitination.
32
What is ubiquitin’s role?
Tags proteins for degradation by the  proteasome in the cytosol.
33
What enzyme degrades ubiquitin-tagged proteins?
Proteasome (ATP-dependent protease complex).
34
How does phosphorylation regulate proteins?
Kinases add phosphates to Ser/Thr/Tyr, altering function (e.g., cell signaling).
35
Where does glycosylation occur? Function?
ER/Golgi (adds sugars to proteins for cell recognition/secretion).
36
What is the function of chaperone proteins?
Assist in proper protein folding and prevent aggregation.
37
What is a signal peptide?
Short N-terminal sequence targeting proteins to the ER for secretion.
38
What is alternative splicing?
Produces different proteins from the same gene by including/excluding exons.
39
What is the role of SRP (signal recognition particle)?
Pauses translation and directs ribosomes to the ER membrane.