Amino acid and protein synthesis test 3 Flashcards

1
Q

AA biosynthesis from alpha ketogluterate

A

glutamate
glutamine
proline
arginine

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2
Q

AA biosynthesis from 3-phosphoglycerate?

A

serine
glycine
cysteine

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3
Q

AA biosynthesis from oxaloacetate

A
aspartate
asparagine
methionine
threonine
lysine
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4
Q

AA biosynthesis from pyruvate

A

alanine
valine
leucine
isoluecine

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5
Q

AA biosynthesis from phosphenolpyruvate and erythrose 4-phosphate

A

tryptophan
phenylalanine
tyrosine

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6
Q

AA biosynthesis from ribose-5-phosphate

A

histidine

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7
Q

T/F DNA is primarily in the nucleosome form?

A

true

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8
Q

what is an intron and exon?

A

introns are non-coding

exons are coding for AAs

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9
Q

All the DNA in mammals codes for proteins T/F?

A

false only 1.5% codes for proteins

25,000 human genes

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10
Q

what is the regulatory/silencer region of DNA?

A

binding of proteins that promote or inhibit transcription

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11
Q

what is the promoter region of DNA?

A

transcription factor and RNA polymerase binding site

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12
Q

what is the open reading frame?

A

AA encoding region containing introns and exons

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13
Q

what is the UTR?

A

untranslated regions necessary for RNA processing

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14
Q

RNA polymerase I

A

synthesizes ribosomal RNA or rRNA

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15
Q

RNA polymerase II

A

synthesis messenger RNA or mRNA

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16
Q

RNA polymerase III

A

synthesis of transfer RNA tRNA

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17
Q

how is DNA read by the RNA polymerase?

A

read 3’-5’

made 5’-3’ (same as non template DNA)

18
Q

what initiates DNA binding of RNA polymerase?

A

transcription factor complexes

19
Q

Negative regulation of DNA transcription

A
  • molecular signal causes repressor to move from operator region
  • molecular signal binds with free repressor which then binds to operator region to inhibit transcription
20
Q

positive regulation of DNA transcription

A
  • enhancement can occur with the removal of an activator(allow binding of RNA polymerase)
  • or the binding of an activator(stabilize RNA polymerase)
21
Q

what are the Three RNA processing steps?

A

addition of 5’ cap
intron splicing
addition of poly A tail
**this is in order of how this happens

22
Q

what is the purpose of the 5’ cap?

A
  • protects mRNA
  • binds to ribosomes to initiate transcription
  • tethers mRNA until translation is complete
23
Q

mRNA splicing

A
  • four classes of introns
  • two are self splicing
  • most introns are not self splicing and require a spliceosomes.
  • introns are released into nuclear space and degraded
24
Q

how does splicing lead to more protein diversity?

A

because splicing happens at different places depending on where it is produced
-thus 1 gene=more than one protein

25
Termination and Poly A tail
``` AAUAAA upstream sequence G and U rich residues downstream protects mRNA tail Anchors mRNA during translation **occurs independent of RNA polymerase ```
26
how does mRNA get out of the nucleus?
binding of protein factors bring the mRNA to nuclear pore and then go off to translation
27
where are the two domains of translation
in the cytosol | and in RER membrane
28
what is the importance of inosinate?
it is very promiscuous and allows for variance in the 3rd codon and allows for resistance to mutation.
29
what are the five steps in translation?
``` activation of AAs initiation elongation termination protein folding ```
30
what occurs in activation
aminoacylating tRNAs (putting the AA on the tRNA)
31
what occurs in initiation
- initiation factors bind to 5' - recruit 40s ribosome complex, which scans mRNA for start codon and the anticodon binds. - poly A tail and 5' keep mRNA in place - then the large 60s ribosome binds * *ATP/GTP hydrolysis drives initiation
32
elongation at the ribosome
- mRNA is read 5'-3' (opposite of RNA polym) - aminoacyl, peptidyl, and exit sites of large ribosome subunit (APE) - poly pep chain is made N->C terminus
33
termination
termination factor causes release
34
proteins made at the endoplasmic reticulum are what kind?
integral membrane proteins intravesicular proteins secreted proteins -primary site of protein modification
35
what is the Signal Recognition Particle cycle?
the SRP on the ER causes the ribosome to associate and make the protein into that site at the RER. -GTP dependent
36
post-translational modifications that occur within the ER
``` protein folding proteolytic cleavage -glycosylation -acetylation -phosphorylation -methylation -acylation ```
37
proteins made at the ER are what kind. (3) of them
integral membrane proteins intravesicular proteins secreted proteins
38
proteins made in the cytoplasmic space are what kind (3) types
nuclear proteins structurally associated proteins membrane-associated proteins
39
how do proteins get into the nucleus?
because they have a nuclear localization sequence on them that recruits other proteins that bring that protein into the nucleus
40
what targets a protein for degradation?
polyubiquitination tags a protein for destruction
41
proteosome degrade what kind of proteins?
degrades cytoplasmic proteins
42
lysosomes degrade what kind of proteins?
degrades vesicular and membrane proteins | *proteins made in the ER