Chapter 10 Flashcards

1
Q

Each amino acid has:

A

3 bases + a codon in the mRNA

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2
Q

tRNAs align amino acids with corresponding codons on the _____ template

A

mRNA

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3
Q

The anticodon loop binds to the appropriate codon by

A

complementary base pairing.

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4
Q

Some tRNAs can recognize more than one mRNA codon, as a result of nonstandard base pairing (wobble) at the ____ codon position.

A

3rd

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5
Q

Name of bacterial ribosome

A

70S

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6
Q

Name of eukaryotic ribosome

A

80s

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7
Q

Ribosomes contain:

A

rRNA and proteins

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8
Q

rRNA is responsible for catalyzing

A

peptide bond formation

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9
Q

mRNAs have noncoding ______ at the ends.

A

UTRs

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10
Q

Most ______ mRNAs are mono-cistronic

A

eukaryote

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11
Q

Most ______ mRNAs are poly-cistronic

A

prokaryote

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12
Q

In both prokaryotes and eukaryotes, translation always starts with:

A

methionine (encoded by AUG)

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13
Q

Initiation codons in bacterial mRNAs are preceded by a __________ sequence, that aligns the mRNA on the ribosome.

A

Shine-Dalgarno

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14
Q

the first step of initiation: a specific initiator methionyl tRNA and the mRNA bind to the _____ ribosomal subunit.

A

small

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15
Q

A group of ribosomes bound to an mRNA molecule

A

polysome.

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16
Q

The initiator methionyl tRNA is bound to

A

eIF2

17
Q

mRNA is brought to the complex by

A

eIF4E.

18
Q

Ribosome scan down the mRNA to identify _____ initiation codon

A

AUG

19
Q

When AUG is identified, _____ triggers the hydrolysis of GTP bound to eIF2.

A

eIF5

20
Q

The initiator methionyl tRNA is bound at the ____ site. The next aminoacyl tRNA binds to the ____ site

A

P, A

21
Q

stop codon examples

A

UAA, UAG, or UGA

22
Q

________ recognize the signals and terminate protein synthesis.

A

Release factors

23
Q

microRNAs are transcribed by:

A

RNA poly II

24
Q

siRNAS are produced from ___________

A

double-stranded RNAs

25
Q

proteins that facilitate folding of other proteins.

A

chaperones

26
Q

Many chaperones were initially identified as

A

heat-shock proteins

27
Q

folding takes place here

A

chaperonin

28
Q

catalyzes disulfide bond formation

A

PDI

29
Q

catalyzes isomerization of peptide bonds that involve proline residues.

A

Peptidyl prolyl isomerase

30
Q

cleavage of the polypeptide chain removes portions such as the initiator methionine from the amino terminus.

A

proteolysis

31
Q

transfer phosphate groups from ATP to the hydroxyl groups of side chains of serine, threonine, or tyrosine.

A

protein kinases

32
Q

Phosphorylation is reversed by

A

protein phosphatases

33
Q

cAMP-dependent protein kinase has:

A

two regulatory and two catalytic subunits.

34
Q

attached to the amino group of the side chain of a lysine residue, then more are added to form a chain.

A

Ubiquitin

35
Q

a large protease complex

A

proteasome.