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
Q

Termination and Poly A tail

A
AAUAAA upstream sequence
G and U rich residues downstream
protects mRNA tail
Anchors mRNA during translation
**occurs independent of RNA polymerase
26
Q

how does mRNA get out of the nucleus?

A

binding of protein factors bring the mRNA to nuclear pore and then go off to translation

27
Q

where are the two domains of translation

A

in the cytosol

and in RER membrane

28
Q

what is the importance of inosinate?

A

it is very promiscuous and allows for variance in the 3rd codon and allows for resistance to mutation.

29
Q

what are the five steps in translation?

A
activation of AAs
initiation
elongation
termination
protein folding
30
Q

what occurs in activation

A

aminoacylating tRNAs (putting the AA on the tRNA)

31
Q

what occurs in initiation

A
  • 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
Q

elongation at the ribosome

A
  • 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
Q

termination

A

termination factor causes release

34
Q

proteins made at the endoplasmic reticulum are what kind?

A

integral membrane proteins
intravesicular proteins
secreted proteins
-primary site of protein modification

35
Q

what is the Signal Recognition Particle cycle?

A

the SRP on the ER causes the ribosome to associate and make the protein into that site at the RER.
-GTP dependent

36
Q

post-translational modifications that occur within the ER

A
protein folding
proteolytic cleavage
-glycosylation
-acetylation
-phosphorylation
-methylation
-acylation
37
Q

proteins made at the ER are what kind. (3) of them

A

integral membrane proteins
intravesicular proteins
secreted proteins

38
Q

proteins made in the cytoplasmic space are what kind (3) types

A

nuclear proteins
structurally associated proteins
membrane-associated proteins

39
Q

how do proteins get into the nucleus?

A

because they have a nuclear localization sequence on them that recruits other proteins that bring that protein into the nucleus

40
Q

what targets a protein for degradation?

A

polyubiquitination tags a protein for destruction

41
Q

proteosome degrade what kind of proteins?

A

degrades cytoplasmic proteins

42
Q

lysosomes degrade what kind of proteins?

A

degrades vesicular and membrane proteins

*proteins made in the ER