ch 7 Flashcards

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1
Q

parts of mRNA

A

5’ UTR
start codon
open reading frame
stop codon
3’ UTR

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2
Q

open reading frame

A

holds instructions to make proteins
only part that gets translated
located in middle of mRNA

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3
Q

start codon

A

where translation starts

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4
Q

stop codon

A

where translation ends

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5
Q

5’ untranslated region UTR

A

not translated
front of mRNA
regulatory information, controls translation

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6
Q

3’ untranslated region UTR

A

not translated
back of mRNA
regulatory information, controls translation

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7
Q

3 main steps in translation

A

initiation
elongation
termination

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8
Q

translation is carried out by ____

A

ribosomes

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9
Q

what are the two main ribosome subunits

A

large and small subunit

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10
Q

translation: initiation

A

initiation factors coordinate its binding

small subunit binds to mRNA
finds start codon

recruits large ribosomal subunit

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11
Q

translation: elongation

A

ribosomes reads open frame and makes polypeptide
RNA nucleotides dictates amino acid sequence
tRNAs decode mRNAs message

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12
Q

T/F: three mRNA nucleotides = one codon

A

true

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13
Q

tRNA parts

A

anticodon
acceptor stem

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14
Q

anticodon

A

binds to codon based on complementary base pairing

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15
Q

acceptor stem

A

where amino acid is attached to tRNA

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16
Q

tRNA charging

A

amino acids is covalently attached to tRNA molecule

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17
Q

aminoacyl tRNA synthetases

A

catalyzes tRNA charging

20 different ones for each amino acids

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18
Q

translation: elongation

A

charged tRNA is brought to the ribosome
ribosome covalently attaches amino acid to polypeptide chain
ribosome translocates forward one codon and repeats

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19
Q

ribosomes have _____ regions where tRNAs bind

A

3

A site
P site
E site

20
Q

Acceptor site

A

where charged tRNAs first enter

21
Q

Peptide site

A

amino acids of tRNA is moved to growing polypeptide
peptide bond forms

22
Q

Exit site

A

where used, uncharged tRNA leaves

23
Q

translation: termination

A

reaches stop codon, translation ends

24
Q

stop codons are bound by ______ instead of tRNA

A

release factor

25
Q

release factor

A

protein that causes mRNA and ribosome to separate

26
Q

translation repressors

A

proteins that bind mRNA and stop translation

sensitive to cellular conditions

27
Q

chaperones

A

proteins that assist in folding other proteins into proper shape

28
Q

three main types of chaperones

A

Hsp70 chaperones
Chaperonins
Protein disulfide isomerases

29
Q

Hsp70

A

heat-shock protein 70
bind new polypeptides
transport them to other places in cell

30
Q

chaperonins

A

large, barrel-shaped proteins that fold other proteins

repeatedly bind and release target protein
causes it to fold
requires energy

31
Q

protein disulfide isomerases

A

enzymes that catalyze the bond between cysteine amino acids across a polypeptide

helps protein fold into proper shape

32
Q

protein cleavage

A

pieces of proteins are cut off
helps them become active

33
Q

proteases

A

enzymes involved in protein cleavage

34
Q

zygomens / proproteins

A

proteins initially inactive by design

cleavage of repressive region activates the protein

35
Q

example of a protein that is activated or inactivated upon binding of small molecules

A

G proteins

36
Q

example of a hormone that regulates proteins

A

estrogen

37
Q

example of a vitamin that regulates proteins

A

vitamin D

38
Q

post-translational modification

A

amino acids of a protein are chemically modified after a protein is built

alters proteins function

39
Q

kinases

A

enzymes that add phosphate groups to proteins

40
Q

conformational change

A

proteins shape changes when modified

41
Q

phosphatases

A

enzymes that remove phosphate groups

42
Q

protein-protein interactions are based on

A

shape and electrical charge of proteins

43
Q

mechanisms of protein regulation

A

small molecule regulators
post-translational modifications
protein-protein interactions
altered cellular location
protein degradation

44
Q

ubiquitin

A

small protein attached to other proteins

takes the proteins to proteasome to be degraded into amino acids

45
Q

ubiquitination

A

attachment of ubiquitins to proteins

46
Q

proteasome

A

degrades proteins into amino acids