4. Translation Flashcards

1
Q

Frame shifting

A

Three different frames to read a codon sequence

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2
Q

Which end is amino acid attached to

A

3’ end

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3
Q

Loading amino acid on tRNA

A
  1. Amino acid is adenylated with ATP (Amino Acid - PO4 - Adenine)
  2. Amino acid is added onto tRNA and AMP is released
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4
Q

Bond type in aminoacyl tRNA

A

Ester bond

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5
Q

Editing tRNA

A

Synthesis site and Editing site - like P and E in Polymerase

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6
Q

Protein synthesis direction (Protein)

A

N terminus to C terminus

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7
Q

Protein synthesis direction (RNA)

A

5’ to 3’

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8
Q

Ribosome size

A

70s - Prokaryote

80s - Eukaryote

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9
Q

Sites in Ribosome

A

A - Aminoacyl
P - Peptidyl
E - Exit

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10
Q

Initiation of Translation

A
  1. Small subunit binds Methionine at P site with elF2 and GTP.
  2. Small subunit recognizes poly-A-tail/5’cap complex
  3. Small subunit binds to 5’ end and moves downstream till it finds the first AUG it finds - Uses ATP to move down
  4. When it reaches AUG, the large subunit binds to the small subunit
  5. GTP is hydrolyzed to remove all the other factors
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11
Q

Elongation of Translation

A
  1. The peptide ester bond between the tRNA and AA at P site is broken and the protein chain is transferred to the tRNA on the A site forming a peptide bond.
  2. This release of energy moves the large subunit a codon downstream
  3. The P site tRNA leaves through the E site and the small subunit follows the large subunit
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12
Q

Proofreading of ribosome

A
  1. tRNAs are bound to EF-tu that carries GTP
  2. The GTP is hydrolyzed, pushing the tRNA onto the A site and swinging around.
  3. If the hydrogen bond is strong enough, the tRNA will stick and the protein will be made
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13
Q

Termination of Translation

A
  1. Release factor binds to A site
  2. The ester bond is hydrolyzed and the protein is released
  3. Everything falls apart
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14
Q

EF-tu

A

Elongation Factor thermo unstable

- Proofreading of tRNA

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15
Q

hsp 70

A

Uses ATP to destabilize the protein

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16
Q

hsp 60

A

A “container” that places protein inside to help re-fold it

Uses ATP to put cap on and off

17
Q

Proteasome

A

Unfoldase ring on each side with protease in the middle

18
Q

Digestion of protein

A
  1. Unfoldase ring recognizes the polyubiquitin chain

2. The protein is pushed into the protease

19
Q

Pulling of Protein into protease

A

The “cap” has six subunits - like helicase

- E from hydrolysis of ATP is used to change the conformation and pull it in

20
Q

Activation of Ubiquitin Ligase

A
  • Phosphorylation by protein kinase
  • Allosteric transition by ligand binding
  • Allosteric Transition by protein binding
21
Q

Activation of Degradation Signal

A
  • Phosphorylation by protein kinase
  • Unmasking by protein dissociation
  • Creation of destabilizing N-terminus (Through hydrolysis)