Chapter 22: Translation Flashcards

1
Q

What is Translation?

A

THe process of turning a transcript into a polypeptide chain using ribosomes

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2
Q

Where does protein synthesis occur?

A

At the Endoplasmic reticulum on ribosomes embedded in the lumen

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3
Q

How is the correct amino acid added to the polypeptide chain?

A
  • tRNA has a complementary sequence to the mRNA
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4
Q

How is it possible there is 64 combinations of three letters but only 20 amino acids?

A

Some amino acids can be coded for by more than one codon. It is called degeneracy

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5
Q

What happens if a missense mutation occurs?

A

It is often a silence mutation because of the genetic code

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6
Q

What is the wobble position and what happens if there is a mutation

A

The wobble position is the third position in a codon and only results in a change of amino acid 25% of the time

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7
Q

What are the following mutations: Transition, silent, frame shift, and nonsense?

A

Transition: Pur replaced by Pur or Pyr by Pyr
Silent: When a mutation results in the same amino acid
Frame shift: when a nucleotide is added or deleted resulting in a shift of the codon reading
Non-sense: premature end

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8
Q

What is an open reading frame?

A

A reading frame without a termination codon among 50+ codons

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9
Q

What is a transversion?

A
  • When a purine is replace by a pyrimidine
    Ex.
    Glu->Val = Sickle cell
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10
Q

If there is 61 possible codons but only 32 tRNAs, How can they be accomidated?

A
  • Third Base of a codon(wobble) can form non-canonical base pair with its complement in tRNA
  • Some tRNA contain Inosinate (I) which can bond with U C and A
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11
Q

What is an overlapping codon?

A

Read the codons in a non-overlapping format

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12
Q

What happens if sequence has an open reading frame?

A
  • A frame without a termination codon 50< codons
  • List all three possibilities for the section
  • Open reading frame must have stop and start
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13
Q

What is involved in protein synthesis?

A
  • Ribosome (rRNA and proteins)
  • mRNA
  • Charged tRNAs (aa activated)
  • Initiation, Elongation, Release factors
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14
Q

What are the five stages of protein translation?

A
  • **Activation of AA **: tRNA is aminoacetylated
  • Initiation of translation: mRNA and aminoacylated tRNA bind to ribosome
  • Elongation: cycle continues till stop codon
  • Termination and ribosome recycling: mRNA and protein dissociate, ribosome recycled
  • Folding and processing: catalyzed by enzymes
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15
Q

What does the tRNA accomplish?

A
  1. Activates an amino acid for peptide bond formation
  2. Ensures appropriate placement of amino acid in a growing chain
    (uses Mg 2+ cofactor)
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16
Q

What is the general composition of the ribosome?

A

A smaller subunit and larger subunit

17
Q

Which rRNA subunit of the ribosome catalyzes the peptide bond formation?

A

30S ribosome subunit

18
Q

What does aminoacylation of tRNA do?

A

Attaches the correct amino acid to the corresponding tRNA

19
Q

How do aminoacyl tRNA make sure they have the right amino acid?

A

Proofreading by aminoacyl-tRNA synthetase

20
Q

Why is the interaction between amino-acyl tRNA synthetase and tRNA referred to as the second genetic code?

A

Because aminoacyl-tRNA synthetase are spcific for the amino acid and tRNA

21
Q

Which amino acid is the first to begin translation in bact, mito, chloro?

A
  • tRNA^fMet
  • Different from methionine found in the middle of the polypeptide chain
22
Q

What is the shiner dalgarno sequence? How does it help alignment of start codon and P site?

A
  • 4-9 purine a few bp upstream of initiation codon
  • Guide mRNA to the correct position on the 30s subunit
23
Q

What are three steps in initiation?

A
  1. IF1, IF2-GTP, IF3 binds to 30S ribosomal subunit
  2. mRNA + fMet bind to shine-Dal aligning sequence, IF3 released
  3. GTP hydrolyzed helps bind 50S, release of IF1 + IF2 form 70S complex
24
Q

Which AA is first to start translation in eukaryotes?

A

Methionine

25
Q

What is the significance of circularization of euk mRNA in translation?

A
26
Q

What are three steps of elongation? (EF-Tu and EF-G)

A
  1. Binding of incoming aminoacyl- tRNA: GTP hydrolyzed EF-Tu GDP released
    • (EF-Tu recycled)
  2. Formation of peptide bond: cataylzed by 23S, amino group of tRNA in A attacks carbonyl tRNA in P site
  3. Translocation: Met moves from P to E causing the rest to follow and continue
    • EF-G is GTP carrier that provides energy for codon shift
27
Q

How do release factors help termination of translation?

A
  • Hydrolyze terminal peptide-tRNA bond
  • Release polypeptide and tRNA from ribosome
  • Cause subunits of ribosome to dissociate so that initiation can begin again
28
Q

What are polysomes?

A

When multiple ribosomes are translating an mRNA

29
Q

What modifications to proteins undergo after termination?

A

Folding and

30
Q

Know how antibiotics inhibit translation. Why don’t they inhibit eukaryotic transcription?

A

Antibiotics dont inhibit eukaryotic transcription because ribosomes are different shapes and sizes than that of bacteria.