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BIOSCI107 - 2021 > CSF: genes to proteins > Flashcards

CSF: genes to proteins Flashcards

(83 cards)

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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
structure
determines function
26
what do DNA mutations affect
ability of protein function
27
what does RNA change about nucleotides
thymine becomes uracil T to U
28
what happens to mature mRNA transcript (ribosome translation)
exits nucleus and is bound by a ribosome
29
tRNA carrys
anticodons
30
what forms between anti codons and codons
hydrogen bonds
31
4 important ribosomal sites:
mRNA binding site A site P site E site
32
A site
holds 'next in line' tRNA
33
P site
holds tRNA carrying growing peptide
34
E site
`tRNA exit from here
35
mRNA binding site
where RNA binds - on the smaller subunit
36
tRNA is
the physical link between the mRNA and amino acid sequence of proteins
37
initiation; what is initiator tRNA
a tRNA carrying a methionine (a starting amino acid)
38
Translation initiation 1/4
1. small ribosomal subunit with bound initiator tRNA binds 5' cap of mRNA
39
Translation initiation 2/4
2. small ribosomal subunit scans downstream to find translation start site AUG
40
Translation initiation 3/4
3. hydrogen bonds between initiator anticodons and mRNA
41
Translation initiation 4/4
4. Large ribosomal subunit binds completing initiation complex
42
what is required for initiation translation
GTP energy - guanosine triphosphate
43
codon recognition
base pairs with the complementary anticodon GTP invested to increase accuracy/efficiency
44
Translocation
move tRNA from A to P site, tRNA in P site moves to E and is released. Energy is required
45
where and how are empty tRNAs filled
in the cytoplasm aminoacyl-tRNA synthase
46
termination translation 1/3
1. ribosome reaches stop codon on mRNA (site A release factor)
47
termination translation 2/3
2. Release Factor promotes hydrolysis, last amino hydrolyzed releasing polypeptides
48
termination translation 3/3
ribosomal subunits and other components dissociate requiring hydrolysis of two GTP molecules. Ribosome can be re-used
49
primary protein bonds
covalent bonds between amino acids - relatively strong
50
primary protein secondary structures
secondary structures start to form as soon as it leaves the ribosome
51
primary is determined by
DNA sequence
52
secondary bonds
weak hydrogen bonds
53
secondary forms
beta sheets and alpha helix
54
tertiary shape
3D stabilized by side chain interactions
55
tertiary TP name
transthyretin polypeptide
56
quaternary structure
transthyretin protein
57
quaternary structure
multiple proteins associated forming a functional protein
58
do all proteins for quaternary structures?
not all do
59
signal peptide
at N terminus of protein
60
SRP
signal recognition particle
61
signal peptides direct ribosomes to rough ER 1
1. polypeptide synthesis begins
62
signal peptides direct ribosomes to rough ER 2
2. SRP binds to signal peptide
63
signal peptides direct ribosomes to rough ER 3
3. SRP binds to receptor protein
64
signal peptides direct ribosomes to rough ER 4
4. SRP detaches and polypeptide synthesis resumes
65
signal peptides direct ribosomes to rough ER 5
5. signal-cleaving enzyme cuts off signal peptide
66
signal peptides direct ribosomes to rough ER 6
6. completed polypeptide folds into final conformation, a secetroy protein is solubilized in lumen, membrane protein remains anchored to the membrane
67
post transitional modifications
addition of groups to a protein
68
addition of phosphate
phosphorylation
69
addition of methyl
methylation
70
addition of acetyl
acetylation
71
addition of Biotin
biotinylation
72
addition of carboxylic acid
carboxylation
73
what can confer activity
phosphorylation and enzyme cleavage
74
ability to interact with other molecules
biotinylation, methylation of histones
75
direct to a particular location
ubiquination
76
mutations
can affect the structure and function of a protein
77
large scale
chromosomal rearrangment
78
small scale alterations
one or a few neucleotides altered
79
point mutations substitutions, are they major or minor
one base replaced by another; minimal to major effect
80
point mutations insertion or deletions, are they major or minor
can cause frame shift; major
81
silent mutations
the mutation occurs however does not affect the outcome of the protein wanting to be made
82
frameshift caused by
insertion or deletion
83
what prime end is more catastrophic
more towards the 5' end is more catastrophic

BIOSCI107 - 2021 (10 decks)

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