tRNA and Codon-Anticodon Recognition Flashcards

1
Q

List the three types of RNA that play major roles in translation.

A
  1. mRNA
  2. rRNA
  3. tRNA
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2
Q

What is the function of mRNA?

A

Codes for proteins

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3
Q

What is the function of tRNA?

A

serve as adapters between mRNA and amino acids during protein synthesis.

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4
Q

What is the function of rRNA?

A

form core of ribosome’s structure and catalyze protein synthesis

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5
Q

What is the function of miRNA?

A

Regulate gene expression.

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6
Q

How do tRNA molecules carry out their adapter function?

A

Carry a specific amino acid, recognizes specific codon, matches amino acid to codon.

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7
Q

What does the anticodon loop of tRNA do?

A

Recognizes codon

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8
Q

What does the 3’ end of tRNA do? WHat is its conserved sequence?

A

Covalently binds to amino acid; CCA

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9
Q

How long is tRNA on average?

A

75 nucleotides.

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10
Q

What are the five modified bases in tRNA?

A

N,N-dimethyl G, dihydro U, pseudouridine, 4-thiouridine, inosine.

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11
Q

What is the purpose of tRNA having modified bases?

A

Helps with codon-anticodon recognition.

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12
Q

Where does tRNA interact with mRNA?

A

Within the confines of the ribosome.

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13
Q

Why is the anticodon said to be the reverse complement to the codon?

A

Complimentary to sequence of codon and written in reversed order

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14
Q

Explain wobble pairing in tRNA.

A

Codon positions 1 and 2 pair with anticoding following Watson-Crick rules. Codon 3 base pairing can wobble, accepting unconventional base pairing.

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15
Q

What can U wobble pair to in eukaryotes and prokaryotes?

A

A, G, or I for both.

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16
Q

What can C wobble pair to in eukaryotes and prokaryotes?

A

G or I for both

17
Q

What can A wobble pair to in eukaryotes and prokaryotes?

A

P: U or I
E: U

18
Q

What can G wobble pair to in eukaryotes and prokaryotes?

A

P: C or U
E: C

19
Q

Which enzyme catalyzes tRNA charging?

A

Aminoacyl tRNA synthetases

20
Q

What is aminoacyl-tRNA?

A

tRNA charged with an amino acid

21
Q

How many aminoacyl-tRNA synthetases are there?

A

20; one for each amino acid

22
Q

How does the aminoacyl-tRNA synthetase charged the tRNA with an amino acid?

A

Covalently links carboxy end of amino acid to 3’-OH of 3’ A of tRNA.

23
Q

What is a class I aminoacylt-tRNA synthetase?

A

Amino acylation at 2’-OH of tRNA adenine. Amino acid then transferred to 3’ OH.

24
Q

What is a class II aminoacyl-tRNA synthetase?

A

Amino acylation directly at 3’-OH.

25
Q

What is the 2 step reaction in tRNA charging?

A
  1. Amino acid covalently linked to ATP, generating aa-AMP
  2. Amino acid transferred from aa-AMP to 3’ adenine of tRNA
26
Q

What are the two sites aaRS uses to selectively attach/remove amino acids?

A
  1. Synthesis site
  2. Editing site
27
Q

What is the role of the synthesis site in aaRS?

A

Amino acids that are too large cannot enter. Anything of the correct size or smaller gets added.

28
Q

What is the role of the editing site in aaRS?

A

Correct amino acid cannot enter the editing site. Incorrect ones enter and get cleaved off.