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BIOSCI107 - 2021 > CSF: genes to proteins > Flashcards

CSF: genes to proteins Flashcards

1
Q

transcription 3 steps

A

initiation, elongation and termination

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2
Q

initiation

A

polymerase binds to promoter

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3
Q

elongation

A

moves downstream through the gene transcribing RNA

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4
Q

termination

A

detaches after terminator reached

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5
Q

template strand

A

3’ to 5’

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6
Q

non-template strand

A

5’ to 3’

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7
Q

what does the TATA box do

A

it is the promoter or start of the transcription

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8
Q

transcription factors

A

bind to DNA

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9
Q

what forms a transcription initiation complex

A

RNA polymerase II and transcription factors

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10
Q

how many nucleotides can RNA polymerase open at a time?

A

10-20

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11
Q

which is stronger hydrogen or phosphodiester bonds?

A

phosphodiester bonds are stronger

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12
Q

elongation (2 points)

A
  1. complementary RNA nucleotides are added to 3’ end of growth transcript
  2. double helix reforms
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13
Q

termination

A
  1. after transciprtion of polyadenylation signal nuclear enzymes release pre-mRNA and RNA then dissociates from DNA
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14
Q

there is less what in RNA synthesis than DNA?

A

less fidelity

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15
Q

capping

A

modified guanine nucleotide added to the 5’ end

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16
Q

tailing

A

50-250 adenine nucleotides are added to the 3’ end

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17
Q

capping and tailing are thought to

A

facilitate export, confer stability, facilitate ribosome bonding in cytoplasm

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18
Q

splicing

A

introns removed from the transcript

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19
Q

exons

A

coding regions (including UTRs)

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20
Q

introns

A

non-coding regions intervening exons

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21
Q

UTR

A

untranslated regions at 5’ and 3’ ends

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22
Q

splicosome

A

Large complex of proteins and small RNAs

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23
Q

Alternative splicing allows for

A

multiple gene products from the same gene

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24
Q

protein sequence determines

A

final function

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25
Q

structure

A

determines function

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26
Q

what do DNA mutations affect

A

ability of protein function

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27
Q

what does RNA change about nucleotides

A

thymine becomes uracil T to U

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28
Q

what happens to mature mRNA transcript (ribosome translation)

A

exits nucleus and is bound by a ribosome

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29
Q

tRNA carrys

A

anticodons

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30
Q

what forms between anti codons and codons

A

hydrogen bonds

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31
Q

4 important ribosomal sites:

A

mRNA binding site
A site
P site
E site

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32
Q

A site

A

holds ‘next in line’ tRNA

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33
Q

P site

A

holds tRNA carrying growing peptide

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34
Q

E site

A

`tRNA exit from here

35
Q

mRNA binding site

A

where RNA binds - on the smaller subunit

36
Q

tRNA is

A

the physical link between the mRNA and amino acid sequence of proteins

37
Q

initiation; what is initiator tRNA

A

a tRNA carrying a methionine (a starting amino acid)

38
Q

Translation initiation 1/4

A
  1. small ribosomal subunit with bound initiator tRNA binds 5’ cap of mRNA
39
Q

Translation initiation 2/4

A
  1. small ribosomal subunit scans downstream to find translation start site AUG
40
Q

Translation initiation 3/4

A
  1. hydrogen bonds between initiator anticodons and mRNA
41
Q

Translation initiation 4/4

A
  1. Large ribosomal subunit binds completing initiation complex
42
Q

what is required for initiation translation

A

GTP energy - guanosine triphosphate

43
Q

codon recognition

A

base pairs with the complementary anticodon GTP invested to increase accuracy/efficiency

44
Q

Translocation

A

move tRNA from A to P site, tRNA in P site moves to E and is released. Energy is required

45
Q

where and how are empty tRNAs filled

A

in the cytoplasm aminoacyl-tRNA synthase

46
Q

termination translation 1/3

A
  1. ribosome reaches stop codon on mRNA (site A release factor)
47
Q

termination translation 2/3

A
  1. Release Factor promotes hydrolysis, last amino hydrolyzed releasing polypeptides
48
Q

termination translation 3/3

A

ribosomal subunits and other components dissociate requiring hydrolysis of two GTP molecules. Ribosome can be re-used

49
Q

primary protein bonds

A

covalent bonds between amino acids - relatively strong

50
Q

primary protein secondary structures

A

secondary structures start to form as soon as it leaves the ribosome

51
Q

primary is determined by

A

DNA sequence

52
Q

secondary bonds

A

weak hydrogen bonds

53
Q

secondary forms

A

beta sheets and alpha helix

54
Q

tertiary shape

A

3D stabilized by side chain interactions

55
Q

tertiary TP name

A

transthyretin polypeptide

56
Q

quaternary structure

A

transthyretin protein

57
Q

quaternary structure

A

multiple proteins associated forming a functional protein

58
Q

do all proteins for quaternary structures?

A

not all do

59
Q

signal peptide

A

at N terminus of protein

60
Q

SRP

A

signal recognition particle

61
Q

signal peptides direct ribosomes to rough ER 1

A
  1. polypeptide synthesis begins
62
Q

signal peptides direct ribosomes to rough ER 2

A
  1. SRP binds to signal peptide
63
Q

signal peptides direct ribosomes to rough ER 3

A
  1. SRP binds to receptor protein
64
Q

signal peptides direct ribosomes to rough ER 4

A
  1. SRP detaches and polypeptide synthesis resumes
65
Q

signal peptides direct ribosomes to rough ER 5

A
  1. signal-cleaving enzyme cuts off signal peptide
66
Q

signal peptides direct ribosomes to rough ER 6

A
  1. completed polypeptide folds into final conformation, a secetroy protein is solubilized in lumen, membrane protein remains anchored to the membrane
67
Q

post transitional modifications

A

addition of groups to a protein

68
Q

addition of phosphate

A

phosphorylation

69
Q

addition of methyl

A

methylation

70
Q

addition of acetyl

A

acetylation

71
Q

addition of Biotin

A

biotinylation

72
Q

addition of carboxylic acid

A

carboxylation

73
Q

what can confer activity

A

phosphorylation and enzyme cleavage

74
Q

ability to interact with other molecules

A

biotinylation, methylation of histones

75
Q

direct to a particular location

A

ubiquination

76
Q

mutations

A

can affect the structure and function of a protein

77
Q

large scale

A

chromosomal rearrangment

78
Q

small scale alterations

A

one or a few neucleotides altered

79
Q

point mutations substitutions, are they major or minor

A

one base replaced by another; minimal to major effect

80
Q

point mutations insertion or deletions, are they major or minor

A

can cause frame shift; major

81
Q

silent mutations

A

the mutation occurs however does not affect the outcome of the protein wanting to be made

82
Q

frameshift caused by

A

insertion or deletion

83
Q

what prime end is more catastrophic

A

more towards the 5’ end is more catastrophic

BIOSCI107 - 2021 (10 decks)

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