Lippincott - Protein Synthesis Flashcards

1
Q

direction of writing of codon

A

5’–>3’

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2
Q

number of base combinations

A

64

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3
Q

number of codons coding for amino acids

A

61

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4
Q

stop codons

A

UAA, UAG, UGA

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5
Q

start codon

A

AUG

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6
Q

protein coded for by start codon

A

methionine

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7
Q

characteristics of genetic code [4]

A

[1] specificity / unambiguity
[2] universality
[3] redundance / degeneracy
[4] nonoverlapping

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8
Q

specificity of genetic code

A

a particular codon codes for only one amino acid

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9
Q

universality of genetic code

A

genetic code found in all organisms

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10
Q

redundance / degeneracy of genetic code

A

a single amino acid has more than 1 coding codon

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11
Q

nonverlapping / commaless

A

code is read from a fixed starting point as a continuous sequence of bases

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12
Q

consequences of altering nucleotide sequence [6]

A
[1] silent mutation
[2] missense
[3] nonsense
[4] triple repeat expansion
[5] splice site mutation
[6] frameshift
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13
Q

silent mutation

A

single nucleotide mutation does not change the amino acid sequence

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14
Q

missense

A

single nucleotide mutation changes amino acid sequence

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15
Q

nonsense

A

single nucleotide mutation produces stop codon

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16
Q

result of nonsense mutation

A

truncated protein

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17
Q

triple repeat expansion

A

amplification of a codon resulting in abnormally high amounts of a single amino acid

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18
Q

splice site mutations

A

failure to correctly splice the protein

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19
Q

frameshift mutation

A

addition or deletion causes change in reading frame and abnormal protein

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20
Q

how is amino acid linked to tRNA

A

carboxyl group of AA is in ester linkage with adenosine of CCA at 3’ end

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21
Q

anticodon

A

complement of codon in mRNA

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22
Q

codon

A

specifies amino acid needed for the sequence

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23
Q

responsible for attachment of AA to tRNA

A

aminoacyl-tRNA synthetase

24
Q

mediators of circularization of mRNA preventing use of incompletely processed mRNA in translation

A

eIF-4 proteins, poly-A binding proteins

25
where do eIF-4 proteins bind?
5' cap
26
prokaryotic ribosomal components
70S = 50S + 30S
27
eukaryotic ribosomal components
80S = 60S + 40S
28
[T\F] ribosomal proteins are more abundant in eukaryotic ribosomes
T
29
products of RER ribosomes
proteins for export
30
products of cytosolic ribosomes
proteins for the cell's own use
31
wobble hypothesis
movement of first anticodon base allows nontraditional pairing with 3rd base of codon, allowing tRNA to recognize more than 1 codon --> more flexible
32
polycistronic synthesis
more than 1 coding region in mRNA
33
monocistronic synthesis
only 1 coding region in mRNA
34
type of coding in eukaryotes
monocistronic
35
Shine-Dalgarno sequence
[1] purine rich sequence located upstream of AUG [2] ribosome can recognize SD sequence [3] binding or ribosome to SD sequence puts coding regions close to AUG
36
direction of movement of ribosome along mRNA in translation
5' --> 3'
37
sites of ribosome
A, P, E
38
ribosome - A site
A (aminoacyl) site; first binding site for charged tRNA - specifies the next amino acid to be added to the chain
39
ribosome - P site
P (peptidyl) site; second binding site for charged tRNA - carries chain of amino acids that have already been synthesized
40
ribosome - E site
E (exit) site; third binding site for charged tRNA - occupied by empty tRNA about to exit
41
elongation in transcription
addition of amino acids to carboxyl end of growing chain
42
elongation factors
mediate the delivery of aminoacyl-tRNA to the mRNA template in the A site
43
responsible for catalysis of peptide bond
peptidyltransferase
44
translocation
process by which the ribosome moves forward 3 nucleotides after creating a successful peptide bond
45
enzyme required for translocation in eukaryotes
EF-2-GTP
46
release factor in eukaryotes
eRF
47
polysomes
complex of 1 mRNA and a number of translating ribosomes
48
important mechanism of translation regulation in eukaryotes
phosphorylation of eIF-2
49
effect of eIF-2 phosphorylation
inactivation of protein, translation is not initiated
50
cotranslational modification of protein
modification while protein is still attached to the ribosome
51
posttranslational modification of protein
modification after synthesis has been completed
52
trimming of proteins
proteins produced as large inactive complexes; cleavage/trimming is required to activate them
53
examples of protein that uses trimming for regulation
inactive trypsinogen trimmed to become active trypsin
54
covalent modifications that may activate or inactivate proteins [4]
[1] phosphorylation [2] glycosylation [3] hydroxylation [4] carboxylation
55
mechanisms of protein folding [2]
[1] spontaneous | [2] nonspontaneous (through chaperone)
56
chaperone
protein that facilitates the proper folding of other proteins