16 Flashcards

1
Q

sHSPs

A

Holdases, Hsp27; bind to unfolded or misfolded proteins in the cell so as to prevent their aggregation; no energy used

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2
Q

a-crystalline abundant in the

A

eye, prevent cataracts

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3
Q

Hsp70

A

switch btwn tightly/weakly binding

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4
Q

Hsp70 cycle driven by

A

ATP

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5
Q

aids of Hsp70 cycle

A

Co-chaperones Hsp40 and nucleotide exchange factors

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6
Q

Hsp70 important for

A

helping nascent proteins fold as they emerge from ribosome

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7
Q

If still misfolded, Hsp70 sends them to

A

Hsp60/Hsp90

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8
Q

Hsp 90

A

dimeric chaperones, switch btwn open/closed states in a cycle
driven by ATP

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9
Q

Hsp90 overexpression leads to

A

cancer

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10
Q

Hsp60

A

GroEL/ES

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11
Q

Hsp60 consumes

A

7 ATP each half-cycle

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12
Q

Hsp60 importance

A

play key roles in translocating proteins through a membrane, such as from the cytosol into the mitochondria

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13
Q

proteasome structure

A

20S core and 2 reg 19S particles (each has a base and lid)

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14
Q

4 activities of proteasome reg particle

A
  • recog of polyubiq substrates
  • deubiq and release of free Ub
  • substrate unfolding
  • translocation of substrate to core particle
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15
Q

Proteasome core particle contains sites of

A

proteolysis

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16
Q

Alzheimer’s mech

A

aggregates of amyloid-β (extracellular) and tau (intracellular) in the cerebral cortex> severe cognitive symptoms (dementia, memory loss)

17
Q

tangles of tau cause

A

chronic traumatic encephalopathy

18
Q

Parkinson’s mech

A

aggregates of
α-synuclein in the substantia nigra (basal ganglia)> controls motor functions and risk/reward mechanisms> rest tremor, slow movements, rigidity; slowed cognition, executive dysfunction

19
Q

diabetes amyloids

A

islet amyloid polypeptides in pancreas

20
Q

atherosclerotic (arteries) plaques: amyloid deposits called

A

apolipoprotein A-I