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FDN1 > Central Dogma > Flashcards

Central Dogma Flashcards

1
Q

methionine aminopeptidase

A

removes Met from proteins; overexpressed in cancerous cells

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2
Q

What protein attaches the tRNA to the A site?

A

EF1 at the expense of one GTP

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3
Q

How many GTPs does it take to charge a tRNA (add aa)

A

2

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4
Q

What does EF2 do?

A

moves the new peptide from the A site to the P site, and release the tRNA in the P site, the expense of one GTP

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5
Q

How does heme regulate globin transcription?

A

Heme inactivates the inhibitor of EF2 - normally a kinase inactivates EF2 but heme prevents that allowing transcription

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6
Q

What are ferritin and transferrin and how are they translationally regulated?

A

Ferritin - binds to Iron
Transferrin - receptor to bring in iron

Both have IRE’s - iron response elements on their mRNA (sites of regulation)

IRE-BP - binding protein that regulates the two mRNAs

When iron levels are low, IRE-BP stbalizes transferring mRNa to increase translation and blocks intiaition on ferritin by binding to the IRE
When iron levels are high, IRE-BP releases from both allowing for the degradation of transferring mRNA and the translation of ferritin

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7
Q

What is the role of BiP?

A

It is a chaperone that prevents transmembrne/secretory proteins from accidentally leaving the ER during translation?

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8
Q

What are the steps of N-linked Glycosylation?

A

N-linked = asaparagine added

- 14 sugar branched oligosaccaride (synthesized in the cytosol and brought in by a oligosaccharyltransferase)

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9
Q

What is a GPI?

A

an anchor for proteins, the sugars that modify proteins can turn into a an anchor and replace the transmembrane portion of protein

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10
Q

What is calnexin?

A

chaperone that checks to see if glycopoteins are properly folded, changes in attached sugars by enzymes are also involved

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11
Q

What are mannosidases?

A

glycoprotein chaperone

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12
Q

How are disulfide bonds formed in the ER lumen?

A

PDI - protein disulfide isomerases

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13
Q

What do glycosidases and glycotrasnferases do?

A

modify sugars on proteins in the golgi and ER

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14
Q

What is O-linked glycosylation?

A

sugar modifications on serine and threonine

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15
Q

What Vesicles are Cathrin coated?

A

Golgi to membrane and lysosome and endocytosis

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16
Q

What vesicles have a COP coat

A

Er to golgi and inter golgi

17
Q

how are vesicles identified?

A

rab proteins (interact w tethering proteins on target)

18
Q

KDEL sequence

A

on resident ER proteins, used to Id what needs to be recycled

19
Q

M-6-phosphate receptor

A

used to take hydrolases to the lysosome, used to get cargo and trigger vesicle formation

20
Q

what protein residues does ubiquitan attach to?

A

lysine

21
Q

ER lumen proteins are re-translocated to allow for degradation

A

sorry not a question plz learn this thx

22
Q

What is ERAD?

A

endoplasmic recticulum associated degredation

basically shit (protein folding lol) in the ER gets fucked up or takes too long so ERAD says bye bye bitch and exports it to the cytosol so it can get ubiquitinated and broken down

23
Q

What is UPR?

A

Unfolded protein response

When there are too many unfolded proteins the body needs to readjust. It increases the transcription of chaperones and stops mRNA transcription till it gets it shit together. If it cant get it together it tells the cell to die. Sounds like me and my life gr8

24
Q

What is the difference between and aggregate and an amyloid?

A

Aggregates are clumps of misoflded proteins where as amyloids are created by a specific alternate folding

25
Q

what can cause misfodled protein aggregates? (4)

A
  1. mutations in protein folding or folding control
  2. translation defects
  3. environmetnal stress
  4. aging
26
Q

What is mTor invovled in?

A

growth factor signaling and autophagy

stimulation = decreased autophagy

27
Q

Which is stronger C-G bonds or A-T?

A

C-G -> 3 instead of 2 hydrogen bonds

28
Q

What are the kinases that recognize DNA damage?

A

ATM & ATR

29
Q

What are the four kinds of DNA repair mechanisms?

A

Base excision repair, nucleotied excision reaprt, non-homologous end joining, and homologous repair

30
Q

The more ____ a molecular, the more energy it has

A

reduced

31
Q

What part of the cell does Gaucher’s disease effect?

A

Lysosome

32
Q

What is the mechanism of Gaucher’s disease?

A

A lysosomal enzyme glucocerebrosidase is dysfunctional so glucocerebrosidase, a breakdown product of cell membranes builds up in macrophages.

33
Q

What organs are affected by Gaucher’s disease?

A

liver, spleen and bone marrow

FDN1 (3 decks)

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