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Cardiovascular and haemotology > protein synthesis > Flashcards

protein synthesis Flashcards

1
Q

what affects the number of RNA polymerases binding DNA

A

transcription factors

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2
Q

how are transcription factors classified

A

according to structure of DNA binding domains
-zinc finger proteins
-helix turn helix proteins
-helix loop helix proteins
-steroid receptors

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3
Q

microbial drug targets in DNA and RNA metabolism, antibiotic and antiviral drug function

A

inhibits DNA metabolism of virus but not host

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4
Q

cancer drug targets in DNA metabolism
what causes mutations
what causes dna damage and how to reduce it

A

anticancer drugs target DNA synthesis, mutations caused by DNA are most common, free oxygen radicals cause DNA damage, reduce free radical levels by antioxidants

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5
Q

what happens in RNA processing

A

addition of 5’ (methyl guanosine) cap, protects mRNA from degradation and helps transcript bind to ribosome during protein synthesis

and splicing of introns

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6
Q

what does the addition of a 5’ cap do

A

protect mRNA from degradation and helps transcripts bind to ribosome during protein synthesis

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7
Q

alternative splicing in eukaryotes vs prokaryotes

A

eukaryotic genes are monocistronic, variants of protein encoded can be produced by alternative splicing

prokaryotic genes are polycistronic, one mRNA can code different proteins

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8
Q

what is alternative splicing

A

genes can form multiple proteins by joining different exon segments in primary transcript

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9
Q

what is the regulation of translation and mRNA decay mediated by

A

untranslated regions of mRNA

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10
Q

what does mRNA do

A

contains code, transcribed from DNA, introns and exons

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11
Q

what does tRNA do

A

carry specific amino acids to corresponding codons in the mRNA using its anti codon, clover shape

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12
Q

what is rRNA

A

site that links amino acids, forms a ribosome

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13
Q

what protein factors are required for peptide synthesis

A

initiation, elongation, termination

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14
Q

describe the codon

A

degenerate- more than 1 codon can code for the same amino acid

universal- codes for the same amino acids in all creatures

specific- particular codon always codes for the same amino acid

non overlapping- code read from a fixed start

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15
Q

describe the 3 main steps of protein synthesis

A

initiation- finds start codon of mRNA and puts first tRNA in P site

elongation- transfer of peptide chain to a new tRNA and moving this new tRNa into P site and putting next codon in the A site

termination- recognition of stop codon in A site, chain dissociates from tRNA, mRNA released from ribosome

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16
Q

what is P and A site and E site

A

P= peptidyl tRNA site, peptidyl tRNA placed before peptide bond formation

A= acceptor tRNA site, aminoacyl tRNA recognises codon

E= uncharged tRNA exiting the ribosome is localised

17
Q

differences in protein synthesis in eukaryotes and prokaryotes

A

-prokaryotic mRNA is polycistronic and eukaryotic mRNA is monocistronic

-start codon is formyl methionine in prokaryotes and amino acid methionine in eukaryotes

-initiation in eukaryotes requires at least 10 initiation factors, 3 in prokaryotes

-prokaryotic ribosome is major target for antibiotics

18
Q

what is polycistronic and monocistronic

A

monocistronic- encodes for a single protein

polycistronic- single mRNA can encode several proteins

19
Q

how is the mRNA codon read

A

5’ to 3’

20
Q

which is the leading strand in DNA

A

3’ to 5’

21
Q

how is DNA read

A

3’ to 5’

22
Q

describe the elongation step

A

-addition of amino acids to carboxyl end
-5’ to 3’ of mRNA
-entry of A site facilitated by elongation factors
-peptidyl transferase catalyses peptide bond formation

23
Q

what catalyses peptide bond formation in elongation

A

peptidyl transferase

24
Q

post translational modifications and explain them

A

glycosylation- addition of specific sugar molecule to protein in ER of golgi, makes glycoproteins

lipidation- anchoring membrane proteins

phosphorylation- switching on/off enzymes and receptors

hydroxylation of lysine and proline- stabilising structure of collagen

25
Q

what are siRNAs and what are they used for

A

synthetic perfectly base pairing microRNA, used to reduce expression of a particular gene

26
Q

what are used for biomarkers

A

microRNAs

27
Q

codons of mRNA

A

AUCG

28
Q

how do mutations form

A

alterations in nucleotide sequence

29
Q

energy sources for mRNA translation

A

ATP and GTP

30
Q
A

Cardiovascular and haemotology (11 decks)

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