Protein Metabolism: Amino Acid and Protein Synthesis Flashcards

1
Q

what are the 2 main sources of amino acids?

A

diet and synthesis

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2
Q

describe the diet as an amino acid source

A
  • essential and non-essential amino acids
  • nitrogen/amine groups
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3
Q

describe synthesis as a source of amino acids

A
  • glucose
  • citric acid cycle carbons from other pathways
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4
Q

___ concentrations are tightly controlled

A

amino acid

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5
Q

T or F:

there is an explicit long-term amino acid storage system

A

false

production of amino acids is dictaed by demands of synthesis since there is no long-term storage system

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6
Q

synthesis of amino acids is a steady state process. what does that mean?

A
  • the body is always producing amino acids
  • specific amino acids are produced as needed based on demands
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7
Q

describe the primary amino acid synthesis pathways. what are the 7 precursors?

A
  • glycolysis
    • 3-phosphoglycerate
    • phosphoenolpyruvate
    • pyruvate
  • pentose phosphate pathway
    • ribose 5-phosphate
    • erythrose 6-phosphate
  • citric acid cycle
    • oxaloacetate
    • alpha-ketoglutarate
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8
Q

glucose provides ___ backbones for amino acid synthesis

A

carbon

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9
Q

only ___ out of the 20 common amino acids are synthesized by humans

A

11

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10
Q

which 2 reaction types are involved in amino acid synthesis?

A

transaminase and single carbon group reactions

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11
Q

name the amino acid biosynthetic families and group them by metabolic precursor. which are essential? nonessential?

A

starred amino acids are essential (acquired from diet), all others are nonessential (produced in humans)

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12
Q

describe the steps of transcription and translation

A
  • ongoing, steady-state process of protein production
  • regulated at several levels
  • limited amino acid palette (20)
  • extensive transcriptional and post-translational processing
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13
Q

describe how DNA is highly organized and compact

A
  • primarily in nucleosome form
  • mitosis forms chromosomes (only in chromosomal state when preparing to undergo division)
  • 46 chromosomes
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14
Q

what are introns and exons?

A
  • intron - non-coding and spliced from RNA
  • exon - encodes for amino acid sequence
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15
Q

what percent of mammalian DNA codes for amino acid chains for proteins?

A

1.5%

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16
Q

approximately how many human genes are there?

A

25,000

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17
Q

DNA encodes for ___, which encodes for ___

A
  • mRNA
  • polypeptides
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18
Q

what is responsible for transcription, post-transcription modification, and translation?

A

DNA, pre-mRNA, and mRNA, respectively

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19
Q

what are regulatory regions?

A

areas from which transcription is initiated and regulated

  • enhancer/silencer - binding of proteins that promote or inhibit transcription
  • promoter region - transcription factor and RNA polymerase binding
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20
Q

what is an open reading frame?

A

amino acid encoding region containing introns and exons

21
Q

what is the UTR?

A
  • untranslated regions necessary for RNA processing
  • do not actually encode for protein
22
Q

what do RNA polymerase I, II, and III synthesize?

A
  • RNA polymerase I - synthesizes ribosomal RNA (rRNA)
  • RNA polymerase II - synthesizes messenger RNA (mRNA)
  • RNA polymerase III - synthesizes transfer RNA (tRNA)

these are multiprotein complexes

polymerases separate DNA strands

transcription initiated by DNA binding

23
Q

how are RNA polymerases recruited to promoter regions?

A

transcription factor complexes will recruit them

24
Q

describe the steps of transcription

25
describe the direction of transcription
26
describe how transcription is negatively regulated at the DNA level
27
describe how transcription is positively regulated at the DNA level
28
after mRNA is produced, what 3 steps occur in RNA processing?
1. addition of a 5' cap 2. intron splicing 3. addition of a poly(A) tail
29
describe addition of 5' cap in mRNA processing
* protects mRNA * bound by ribosomes to initiate translation * cap-binding complex tethers the mRNA until transcription is complete
30
describe the intron splicing step of mRNA processing
* four classes of introns encoded into RNA * 2 classes are self-splicing * most introns are spliced by spliceosome complexes * spliceosomes associate with RNA polymerase * introns are released into the nuclear space and degraded
31
splicing variance creates different nRNAs and products. as an example, what proteins are produced from the same primary transcript (gene) in the thyroid vs. brain?
* thyroid - calcitonin * brain - CGRP
32
describe the termination and poly(A) tail step in mRNA processing
* highly conserved cleavage sequence * AAUAAA upstream sequence * G and U rich residues downstream * polyadenylate polymerase adds 80-250 A residues * protects mRNA tail * anchors mRNA during translation * **poly A addition occurs independent of RNA polymerase**
33
describe nuclear export
transports mRNA to the cytoplasm for translation
34
translation can occur in which two places?
free in cytosol or in the ER
35
what are mRNA codons?
* triplet of nucleotides that specify an amino acid in the protein polypeptide chain * determine amino acid sequence * mRNA is composed of codons
36
which amino acids are stop codons? which one is the initiation codon?
* stop: UAA, UAG, UGA * initiation: AUG (methionine)
37
what does inosinate do?
allows for variance in last (3rd) codon\*\*, providing resistance to mutation \*\*degenerate code, due to wobble (3rd) base
38
describe the steps of translation
39
what is responsible for activation?
aminoacylating tRNAs
40
what happens in initiation?
* building of the ribosomal complex * ATP/GTP hydrolysis drives initiation * 5' cap and 3' end are bound in place; without this, initiation cannot happen know this general process
41
describe elongation
* start codon binds to mRNA and peptidyl domain * amino acids move through aminoacyl until matching code is produced * mRNA read 5' to 3' * polypeptide chain: N to C terminus * GTP hydrolysis dependent
42
describe termination
eRF3 - eukaryotic releasing factor
43
synthesis location affects protein targeting and transport. describe the effects of protein targeting and transport at the endoplasmic reticulum.
* integral membrane proteins * intravesicular proteins * secreted proteins * signal recognition particle (SRP) cycle
44
describe post-translational modifications. where do they occur?
* occur in the ER 1. protein folding and structure 2. proteolytic cleavage 3. post-translational modifications: * glycosylation * acetylation * phosphorylation * methylation * acylation
45
describe glycoprotein formation in the ER
46
synthesis location affects protein targeting and transport. describe the effects of protein targeting and transport in the cytoplasmic space.
* nuclear proteins * structurally associated proteins * membrane-associated proteins
47
what do the proteosome and lysosome do?
degrade proteins
48
what is ubiquitin's role in degradation of proteins?
it can target proteins for destruction (usually requires multiple ubiquitins to bind)
49
describe the proteins that proteosomes and lysosomes degrade
* proteosome: degrades cytoplasmic proteins * lysosome: degrades vesicular and membrane proteins