Week 2 Richter Lectures Flashcards

1
Q

a group of genes, regulated together by transcription from a single promoter that produces polycistronic mRNA

A

operon

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2
Q

repressor binds to operator= what to transcription

A

inhibits

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3
Q

what is used to break down lactose

A

lac operon (found in prokaryotes)

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4
Q

Trp bound to repressor causes what to transcription

A

inhibits (Trp operon-found in prokaryotes)

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5
Q

acetylation of histones does what

A

turns on gene expression

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6
Q

methylation of histones does what

A

turns off gene expression (silences it)

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7
Q

what often happens to cancer (acetylation and methylation example)

A

oncogenes need to be methylated (to silence the gene)

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8
Q

drug used in anti-cancer chemotherapy that can reverse gene silencing, reduce proliferation, and trigger apoptosis

A

Vorinostat (drug that inhibits HDAC)

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9
Q

remove acetyl groups from chromatin, which often silences gene expression

A

histone deacetylases (HDACs)

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10
Q

what happens when gene expression is activated that should instead be silenced

A

cancer

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11
Q

if these get methylated, they won’t be able to stop cancer

A

tumor suppressors

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12
Q

3 functions of transcription factors

A
  1. DNA binding domain
  2. dimerization domain
  3. activation domain
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13
Q

a DNA-binding domain that allows TFs to insert themselves into grooves of DNA; Cys or His residues bound to Zn2+

A

Zinc finger

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13
Q

what receptors are basically transcription factors

A

nuclear receptors

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13
Q

DNA binding domain that has + and - charge by ionic interaction

A

basic domain

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13
Q

mutation of Vitamin D receptor leading to vitamin D deficiency

A

Rickets

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13
Q

mutation in thyroid hormone receptor leads to low T3 and thyroxine

A

Hypothyroidism

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13
Q

mutation of cortisol receptor leading to high levels of corticosteroids

A

Cushing’s Disease

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13
Q

nuclear receptor used in birth control (combination of 2)

A

estrogen/progesterone

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14
Q

mutation of retinoic acid receptor; can cause developmental defects in embryo and fetus

A

retinoic acid derivatives

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14
Q

used for acne and is contradicted during pregnancy

A

retinoic acid

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15
Q

2 dimerization domains

A

leucine zipper and HLH (helix-loop-helix) domain

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16
Q

All transcription factors are what

A

dimers

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17
Q

leucine residues are where on the helix (for leucine zipper)

A

on the same face

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18
Q

transcription factor class that control fundamental architectural plan of developing embryo

A

helix-turn-helix

(from Hemeobox (Hox) genes)

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19
Q

key process in gene silencing and defense against viral infections

A

RNA interference (RNAi)

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20
Q

main player in RNA interference (gene silencing)

A

miRNA

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21
Q

activates and cleaves mRNA during miRNA synthesis and gene silencing

A

RISC (RNA induced silencing complex)

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22
Q

regulated process during gene expression that results in a single gene coding for multiple proteins

A

alternative splicing

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23
Q

atleast one specific what is required per amino acid during translation

A

tRNA

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24
Q

what is the form of tRNA ready to be used in translation; and connects to amino acid

A

aminoacyl-tRNA

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25
Q

used as a signal initiation of translation; how the cell knows this RNA needs to be translated

A

7-methyl guanosine cap

26
Q

a longer polyA tail means what for translation

A

most likely to happen

27
Q

Initiation step of translation:

A
  1. binding of methyl cap
  2. joining of elF4B
  3. 43S complex
  4. joining of 60S with 43S at start codon (starts when it hits its first AUG)
28
Q

elongation of translation sites:

A

A: recruits incoming aminoacyl tRNAs
P: growing tRNA (from P to A)
E: exit site (for empty tRNA)

29
Q

many mRNAs have multiple _____ bound that allows translation of many proteins

A

ribosomes

30
Q

this happens when the release factor enters the A site

A

termination of translation

31
Q

this antibiotic binds to 30S subunit and causes misreading of genetic code; also inhibits initiation

A

aminoglycoside (streptomycin/gentamicin)

32
Q

this antibiotic binds to 30S acceptor site (A site) and is just in the way

A

tetracycline

33
Q

this antibiotic binds to 50S subunit and inhibits peptide bond formation

A

chloramphenicol

34
Q

this antibiotic binds to 50S and blocks transferase reaction (inhibits enzyme that catalyzes formation)

A

erthromycin

35
Q

this antibiotic binds to A site and acts as peptidyl acceptor- aborting elongation (blocks elongation)

A

puromycin

36
Q

what blocks translation by inhibiting mTOR (mammalian target of rapamycin); inhibiting elF4E inhibits translation; also prevents blood vessel walls from thickening after angioplasty

A

rapamycin

37
Q

addition/removal of AA’s through signal sequence(marks protein for secretory pathway)/ubiquitination (degradation by proteasome)

A

post-translational modification

38
Q

4 steps of post-translational modification

A
  1. add/remove AA’s
  2. add carbohydrates
  3. add lipids
  4. reversible regulation through chemical modifications
39
Q

what post-translational modification is essential for proper protein folding

A

N-glycosylation

40
Q

addition of lipids to protein through post-translational modification

A

myristylation

41
Q

amino acids used in phosphorylation during post-translational modification

A

Ser
Thr
Tyr

42
Q

amino acids used in hydroxylation during post-translational modification

A

pro
lys

43
Q

methylation of histones

A

inhibits transcription

44
Q

acetylation of histones

A

promotes transcription

45
Q

lowers energy required for transition state (free energy of activation); increases rate of rxn

A

enzyme

46
Q

rxn speed is increased dramatically when you introduce more ____

A

substrate

47
Q

this alters enzyme activity and is different in different areas of the body

A

pH

48
Q

extreme temperatures (high and low) do what to enzymes

A

inactivate them

49
Q

substrate concentration at 1/2 vmax; similar to ligand concentration needed to occupy 50% of binding sites

Measure of AFFINITY

A

Km; Kd

50
Q

rxn speed is proportional to substrate concentration

A

first order

51
Q

independent of substrate concentration

A

zero order

52
Q

drug that competes with HMG-CoA (substrate at the active site); more drug than substrate leads to enzyme activity reduced

A

statin

53
Q

shift of curve to the right (Km increases-add more substrate to get back to Km)

A

competitive inhibition

54
Q

inhibitor does not compete with substrate at binding site; amount of active enzyme has decreased (vmax decreases)

A

noncompetitive

55
Q

example of noncompetitive inhibitor

A

lead

56
Q

lead being a noncompetitive inhibitor of ferrochelatase impairs heme synthesis and leads to what

A

anemia

57
Q

inhibitor only binds to enzyme-substrate complex; vmax and Km decrease

A

uncompetitive enzyme inhibition

58
Q

example of uncompetitive inhibitor (immunosuppressant); inhibits IMP dehydrogenase (B and T cells use this process)

A

mycophenolate

59
Q

similar to noncompetitive; vmax decreases and Km stays the same

A

irreversible inhibition

60
Q

organophosphorus pesticides leads to inhibition of acetylcholinesterase= SLUDGEM

A

irreversible inhibition

61
Q

(drug) proton pump inhibitor; type of irreversible inhibition

A

omeprazole

62
Q

can change Vmax or Km

A

allosteric regulators

63
Q

AMP, GMP, IMP are heterotropic what

A

allosteric inhibitors

64
Q

if IMP, GMP, and AMP are abundant in the cell; what feedback happens

A

negative

65
Q

how cells even out substrates and products

A

+ and - feedback loops

66
Q

what reduces DNA synthesis and explains toxicity of increased levels of dATP in adenosine deaminase deficiency

A

binding of dATP to allosteric sites on enzyme inhibiting enzyme activity

67
Q

all CK in the brain is what isoform

A

BB

68
Q

all CK in skeletal muscle is what isoform

A

MM

69
Q

in cardiac muscle, 1/3 of CK is ___ and the rest is_____

A

MB; MM

70
Q

enzyme indicator that cardio conversion (after myocardial infarction) was successful

A

MB (returns to normal value-decreases)

71
Q

antibiotic that binds at A site and acts as a peptidyl acceptor

A

puromycin