week two, post-translational modifications Flashcards

1
Q

where are proteins modified after translation

A

Endoplasmic reticulum or Golgi apparatus

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2
Q

what are the two main types of Post-translational modification

A

proteolysis and the covalent addition of molecules

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3
Q

what are the main functions of proteolysis ?

A
  • Makes isoforms of proteins from single mRNA
  • Convert protein to its active form
  • Enhances proper protein folding
  • Enhances insertion of protein to membrane or lumen of organelles
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4
Q

what are the main functions of the addition of covalent molecules to proteins?

A
  • Enhance or disrupt interaction with other proteins
  • Enhances stability or degradation
  • Enhances transportation
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5
Q

Why is insulin produced in an inactive state ?

A

allows it to travel to its target tissue without having an immediate effect.

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6
Q

describe insulin matuaration

A
  • From N term preproinsulin consists of a signal sequence, chain B, Chain C and chain A
  • proinsulin is made when the signal sequence is removed from the N term
  • Chain C is then removed to form active insulin, leaving chain B and A connected by di sulphite bridges.
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7
Q

what does the Acetylation of histones cause

A

causes relaxation of the nucleosome making DNA more accessible

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8
Q

what does the Methylation of histones cause

A

causes condensation of the nucleosome making DNA inaccessible

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9
Q

Phosphorylation

A

addition of phosphate group

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10
Q

what enzymes add phosphate groups

A

Kinases

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11
Q

what enzyme removes phosphate groups

A

phosphatase

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12
Q

Ubiquitylation

A

addition of Ubiquitin

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13
Q

what does ubiquitylation do

A

Tags protein for degradation, mostly uses to discard faulty proteins

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14
Q

Glycosylation

A

addition of sugar moiety side chains of amino acid

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15
Q

N-linked glycosylation

A

addition of sugar moiety to Nitrogen of Asparagine

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16
Q

what is N-linked glycosylation important for ?

A

protein folding

17
Q

where does N-linked glycosylation occur

A

initially in the ER and is refined in the Golgi

18
Q

O-linked glycosylation

A

addition of sugar moiety to the Oxygen atom of Serine and Threonine

19
Q

what does O-linked glycosylation do

A

it is complimentary to phosphorylation and enhances protein-protein interaction

20
Q

where does O-linked glycosylation occur

A

mostly in the cytoplasm