Protein translation and post-translational modification Flashcards

1
Q

explain why some antibiotics inhibit protein synthesis in prokaryotes but not eukaryotes

A
70s ribosomes - prokaryote 
80s ribosomes - eukaryote 
have different RNA and proteins
antibiotic selectivity inhibits AA 
natural products of bacteria/fungi - give them a selective advantage
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2
Q

features of proteins that allow them to enter the secretory pathway

A
signal sequence - hydrophobic AA 
sequence recognition 
halt translation until bound to RER 
grow into lumen 
cleavage by signal peptidase 
co-translational - as soon as translated it is about to be cleaved
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3
Q

summarise the ways in which newly-synthesised proteins can be post-translationally modified

A
phosphorylation 
proteolytic cleavage - insulin A--B (secretory vesicle) 
lipid groups - phenylation/acylation 
hydroxylation - collagen 
disulphide bond formation (insulin)
addition of carb (glycosylation) 
addition of phosphate (phosphorylation)
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4
Q

describe the 40s subunit of ribosomes

A

the rna folds in on itself

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5
Q

What is the direction of protein translation

A

mRNA transcribed in 5’-3’

N-C terminus

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6
Q

describe the structure of mRNA

A

5’ cap - 7-methyl guanosine - entry site for ribosome
poly-A - protect from degradation
UTR (untranslated regions) involved in regulation of translation/stability

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7
Q

how many codons are there

A

64
common AA several codons
because widely used

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8
Q

describe the reading of mRNA

A

ribosome scans from 5’ of mRNA
translations starts at AUG
continues in frame
stops at first in frame stop codon

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9
Q

describe tRNA

A
transporters of AA to ribosome 
single strand 
fold in tertiary structure 
anticodon exposed 
antiparallel binding
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10
Q

describe the function of aminoacyl tRNA synthetases

A
1 for each AA 
important in fidelity of translation  - selectivity for correct AA and tRNA, hydrolysis of incorrect aa-tRNA 
help tRNA 
hook AA to tRNA 
AA -- E-AMP-AA
complex come to specific tRNA - recognition step
remove AMP and enzyme 
hooked to side at 3' 
ready to go to ribosomes
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11
Q

describe initiation of translation

A
  • dissociation of ribosome subunits
  • assembly of pre-initiation complex - e1F4E and e1F4G bind to cap and are recognised by 40s/Met-tRNA/eIF2
  • binding of mRNA to pre-initiation complex - Met binding sets frame of translation
  • binding of 60s subunit - GTP-GDP + Pi - ensure binding to correct base pair
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12
Q

describe elongation of translation

A

factors movement of ribosome using GDP

  • bind tRNA in A site on ribosome in frame with met
  • peptidyl transferase catalyses peptide bond between 2 AA
  • Translocation of peptidal tRNA to P site - elongation factors promote movement with GTP
  • new cycle
  • EFs - GTP hydrolysis provide pauses to increase accuracy of translation
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13
Q

describe termination of translation

A
  • recognise stop codon - hydrolysis (peptidyl transferase) - release factors bind to empty A site
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14
Q

streptomycin

A

inhibit initiation

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15
Q

tetracycline

A

inhibit aa-tRNA binding

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16
Q

erythromycin

A

inhibits translocation

17
Q

chloramphenicol

A

inhibits peptidyl transferase

18
Q

puromycin

A

terminates elongation prematurely