Protein Translation Flashcards

1
Q

Define Translation

A

Biological polymerization of amino
acids into polypeptide chains

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2
Q

Translation requires what 4 features?

A
  • Amino acids
  • mRNA
  • Ribosomes
  • tRNA
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3
Q

Define Transfer RNAs

A
  • Adapt genetic information present as specific triplet codons in mRNA to corresponding amino acid
  • tRNA anticodons complement mRNAs
  • tRNAs carry corresponding amino acids
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4
Q

Prokaryote ribosomes are ___S.

Eukaryote ribosomes are ___S.

A

Prokaryote: 70S

Eukaryote: 80S

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5
Q

Explain rDNA

A
  • rRNA genes
  • Moderately repetitive DNA fraction present in clusters at various chromosomal sites
  • Each cluster contains tandem repeats separated by noncoding spacer DNA (These spacer regions are used to identify the type of organism we have)
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6
Q

Why do we even need these repetitive regions present?

A

We need ribosomes present all the time because we make a plethora of different molecules. We ALWAYS need to have ribosomes present

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7
Q

Define tRNA

A
  • Small in size and very stable
  • 75–90 nucleotides
  • Transcribed from DNA
  • Contain posttranscriptionally modified bases
  • tRNAs have a cloverleaf structure
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8
Q

What is the 3 bases that will be found always at the 3’ end of tRNA

A

CCA

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9
Q

Explain Anticodon

A
  • tRNA has anticodon that complementarily base-pairs with codon in mRNA
  • Corresponding amino acid is covalently linked to CCA sequence at 3′ end of all tRNAs
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10
Q

Explain Aminoacylation

A
  • Known as tRNA charging
  • Before translation can proceed, tRNA molecules must be chemically linked to respective amino acids
  • Aminoacyl tRNA synthetase: Enzyme that catalyzes aminoacylation
  • 20 different synthetases, one for each amino acid
  • Highly specific; recognize only one amino acid
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11
Q

What is the difference between prokaryotes and eukaryotes in terms of the methionine.

A

methionine that starts as first is a formylmethionine. ONLY the first one in bacterial synthesis. In eukaryotes, it is just methionine

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12
Q

Undertsand the site of the rubosome in terms of A, P, and E site

A

A site: Aminoacyl attachment

P site: peptide bond formation

E: Exit site

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13
Q

For the 3 stop codons, is there a tRNA corresponding with the anticodon?

A

NO!

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14
Q

What 6 things does Initiation require?

A
  • Small and large ribosomal subunits
  • mRNA molecule
  • GTP
  • Charged initiator tRNA
  • Mg2+
  • Initiation factors
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15
Q

T/F: Only the initiator sequence AUG will go in through the P site. Everything else goes in through the A site

A

TRUE!

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16
Q

Explain Shine-Dalgarno sequence

A
  • AGGAGG
  • Precedes AUG start codon in bacteria
  • Matches up with the 16S rRNA starting initiation
17
Q

What makes up the initiation complex of prokaryotic translation

A
  • Small ribosomal subunit + initiation factors + mRNA at codon AUG
  • Combines with large ribosomal subunit
18
Q

Polycistronic messages are always in what type of system?

A

Prokaryotic because we make multiple “messages” aka genes that are coded

19
Q

In Eukaryotic genes, we have what type of system?

A
  • Monocistronic
  • Only one gene is regulated by that one operon.
20
Q

What are the 3 STOP codons?

A

UAA

UGA

UAG

21
Q

What is 23S rRNA known as?

A
  • Ribozyme with the catalytic activity of peptidyl transferase
  • Catalyzes peptide bond formation between amino acid on tRNA at A site and growing peptide chain bound to tRNA in P site
22
Q

What are GTP-dependent release factors?

A

Stimulates hydrolysis of polypeptide
from peptidyl tRNA—released from
translation complex

23
Q

What are Polysomes (or polyribosomes)

A
  • mRNAs with several ribosomes translating at once
  • As mRNA passes through ribosome, its free to associate
    with another small subunit
24
Q

Every amino acid has what properties?

A
  • Carboxyl group
  • Amino group
  • R (radical) group bound to central carbon atom
25
Q

How is a peptide bond formed?

A

Dehydration (condensation) reaction between carboxyl group and amino group

26
Q

Explain the primary structure of a protein

A

Only sequence of amino acids

27
Q

Explain the Secondary protein structures

A

a-helix and B-pleated sheets

28
Q

Explain the Tertiary Protein structures

A

3-D conformation of a SINGLE protein

29
Q

Explain the Quaternary structure

A

Composed of more than one polypeptide chains