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Aging > Protein Homeostasis and Aging > Flashcards

Protein Homeostasis and Aging Flashcards

1
Q

Entire set of proteins expressed by a genome, cell, tissue, or organism under defined conditions

A

proteome

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2
Q

a state of dynamic equilibrium where protein synthesis and folding are balanced with protein degradation

A

protestasis

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3
Q

experimented with urea and found that all information required for protein folding is
provided by the amino acid sequence

A

Anfinsen’s experiment

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4
Q

levinthal paradox

A

demonstrates that a purely random search for the correct conformation can’t work

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5
Q

folding intermediates

A

accelerate folding

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6
Q

a chaperone

A

a protein that interacts with, and aids in,
the folding or assembly of another protein without being part of its final structure

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7
Q

most chaperones are

A

hsps, their synthesis is induced by stress

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8
Q

how do chaperones work

A

Many chaperones act by binding exposed hydrophobic regions to prevent nonnative
interactions and protein misfolding

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9
Q

atp dependent
Ubiquitous class of chaperones; constitutively
expressed and stress-induced members

A

Hsp70s

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10
Q

hsp70 open state

A

atp bound

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11
Q

hsp70 closed state

A

adp bound

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12
Q

hsp40 co-chaperones with __ to do ___

A

with hsp70 to deliver misfolded substrates

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13
Q

hsp90s

A

Regulation of protein complex assembly and
translocation

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14
Q

which hsp is highly expressed in all species

A

hsp90s

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15
Q

which hsp stabilizes a number of proteins required for tumor growth, investigated as anti-cancer drugs

A

hsp90s

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16
Q

whose activity is coordinated by stress inducible phosphoprotein 1 (STl1)

A

hsp70 and hsp90

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17
Q

which hsp is involved in disaggregation

A

hsp100s

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18
Q

disaggregase yeast

A

hsp104

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19
Q

mammalian disaggregase

A

HSP110 +HSP40 +HSP70

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20
Q

which hsps are involved in prevention of aggregation

A

hsp 60s and shsps

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21
Q

how do smallHSPs work

A

surround other proteins to control and sequester aggregates
act early

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22
Q

chaperone functions

A

Folding/refolding of de novo and
misfolded proteins
Regulate protein complex formation
Mediate the response to proteotoxic
stress (heat shock, oxidative stress,
heavy metals, etc.)

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23
Q

heat shock response

A

Cellular response to proteotoxic stressors
aimed at restoring protein homeostasis.

results in increased expression of chaperones

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24
Q

HSF-1 is a…

A

transcription factor

25
Q

hsf-1 process

A

triggered by an increase in unfolded proteins
chaperones are titrated away proteins
Hsf1 homo-trimerizes and translocates to the
nucleus to promote transcriptional activity of
HSR gene

26
Q

secreted or proteins with hydrophobic domains can be properly folded and targeted here
without aggregating.

A

ER

27
Q

ultimate goal of the UPRER response

A

decrease the concentration of misfolded proteins in the ER.

28
Q

what is UPRer response

A

a signaling pathway which relieves stress by
selective gene upregulation and other mechanisms

triggered by increase of unfolded proteins

29
Q

programmed ER stress leads to

A

apoptosis

30
Q

oligomerizes, autophosphorylates and
activates its RNase domain to remove an intron from XPB-1 mRNA to facilitate its translation. XPB-1 then binds to specific promoters to activate transcription of UPR genes

A

IRE1

31
Q

phosphorylates eIF2α to block the
formation of ribosomal pre-initiation complex and to attenuate translation, while at the same time preferentially translate the ATF4 transcription factor

A

PERK

32
Q

migrates to the Golgi upon UPR induction,
where it is cleaved; it moves out to the nucleus and activates transcription from ER-stress responsive promoters.

A

ATF6

33
Q

mitochondria has its own

A

UPR

34
Q

Within a single cell, the mitochondria can signal to change

A

nuclear transcription

35
Q

RNAi disruption of a mitochondrial ETC gene, cco-1 can induce

A

UPR mito

36
Q

In C. elegans it is possible to knock down

A

genes in specific tissues

Strategy: express a hairpin (HP) ds RNA; inverted repeat of a sequence can self anneal into a double stranded RNA

37
Q

Cell non-autonomous =

A

inactivate gene in one cell but see the effect in another

38
Q

Proteo-stress in the mitochondria of one cell (neuron) can be communicated to

A

induce protein-folding defense in another cell (intestine)

39
Q

Ubiquitin proteasome system (UPS)

A

Degrades unnecessary or damaged proteins
through proteolytic activity of proteasomes

40
Q

Autophagy

A

Degrades unnecessary or dysfunctional
cellular components through the actions of
lysosomes (organelles, proteins, etc.)

41
Q

Ubiquitin itself contains 7 lysine residues to
which another ubiquitin can be ligated, forming —

A

polyubiquitin chains

42
Q

recognizes Lys-linked chains of 4 or more
ubiquitins

A

proteasome

43
Q

Ubiquitin activating enzyme

A

E1

44
Q

Ubiquitin conjugating enzymes

A

E2

45
Q

Ubiquitin ligases

A

E3

46
Q

Ubiquitin process

A

Ubiquitin gets ligated to a substrate for degradation (more than once)
Polyubiquitin directs to the proteasome, which deubiquitinates it, unfolds it, and degrades it

47
Q

hollow and provides a cavity with proteolytic
activity

A

Proteasome 20S core particle

48
Q

recognize ubiquitinated proteins and regulate
transfer to the catalytic core.

A

Proteasome 19S regulatory caps

49
Q

20s core α subunits

A

interact with the 19S caps and form a gate that blocks unregulated access to the core

50
Q

20s core b subunits

A

have the protease activity

51
Q

19S regulatory particle

A

binds atp
ATP hydrolysis provides energy for substrate
unfolding (required for transfer into narrow
core)
Removes ubiquitin chain from substrate
Opens gate provided by α subunit
in core

52
Q

Ubiquitin proteasome system

A

Degrades unnecessary or damaged
proteins through proteolytic activity of
proteasomes

53
Q

Autophagy

A

Degrades unnecessary or dysfunctional
cellular components through the actions
of lysosomes

54
Q

Lysosomes are

A

acidic

55
Q

Macroautophagy

A

Removes damaged organelles, aggregated
proteins, lipids, and more
* Double membrane structure
fuses

56
Q

Microautophagy

A
  • Direct engulfment of cytoplasmic material
    by lysosomes (organelles, proteins)
  • Lysosomal membrane invaginates and
    engulfs the cytoplasmic material directly
57
Q

Chaperone-mediated autophagy
(CMA)

A

Lysosomal degradation of individual proteins
* Selective autophagy pathway
– Hsc70 recognizes KFERQ-like motif

58
Q

Chaperone and Hsf1 over-expression

A

improves lifespan

Aging (9 decks)

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