Protein synthesis Flashcards

1
Q

Describe the structure of mRNA at the start of translation

A
5' 7-methylguanosine cap
5' UTR (untranslated region)
Start codon (AUG)
Stop codon 
3' UTR
Poly-A tail
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2
Q

What is the most common start codon, and what does it code for?

A

AUG

Methionine

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3
Q

How many codons are there for how many amino acids?

What can DNA be described as as a result?

A

64 for 20

Degenerate

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4
Q

What are the 3 stop codons?

A

UAA
UAG
UGA

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5
Q

What direction is mRNA translated?

A

5’ to 3’

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6
Q

What is the entry site for a ribosome?

A

7-methylguanosine cap

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7
Q

What is the difference between ribosomes in eukaryotes/prokaryotes?

A

Eu: 80s ribosomes, 49 proteins
Pro: 70s ribosomes, 33 proteins

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8
Q

What does the difference in eu/pro ribosomes allow the use of?

A

Antibiotics secreted from bacteria/fungi which only act on prokaryotes
They give a selective advantage.

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9
Q

Name the three stages of translation

A
  1. Initiation
  2. Elongation
  3. Termination
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10
Q

Where does an amino acid bind to tRNA?

A

3’

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11
Q

Which enzyme ‘picks up’ an amino acid, and binds it to tRNA?

How does it work?

A

aminoacyl tRNA synthetase - specific to each amino acid.
Amino joined to enzyme using ATP. Forms E-AMP-Aminoacid
tRNA removes enzyme and AMP

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12
Q

What is the first stage of initiation?

A

40s + 60s subunits dissociate into cytoplasm looking for mRNA

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13
Q

What happens when the 40s subunit locates mRNA?

A

Preinitiation complex assembles.

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14
Q

What does the preinitiation complex consist of?

A

Met-tRNA, eIF’s 40s subunit

Met as its always the first AminoA

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15
Q

What is eIF?

A

An initiation factor

Group of proteins

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16
Q

What happens to the preinitation complex?

A

The 60s subunit binds.

A full ribosome is formed.

17
Q
What do eIFs do? 
Name them (3)
A

eIF 4E + 4G bind to 5’ cap

eIF2 contains GTP which is hydrolysed to bind 60s when AUG is found

18
Q

Name the 2 sites of a ribosome in elongation

A

P site - on the left (peptidal)

A site on the right of the P site (amino acyl)

19
Q

Describe elongation (3 steps)

A
  1. Next tRNA binds to a site
  2. Peptide bond formed between 2 amino acids on P and A sites by peptidyl transferase.
  3. Translocation of tRNA from A to P, (previous P dissociates)
    Repeat
20
Q

How quick is elongation?

A

15 codons/second

21
Q

Describe termination (3 steps)

A
  1. Stop codon recognised
  2. Release factors bind to empty A site.
  3. Protein dissociates, ribosome dissociates
22
Q

What is a polyribosome?

A

Several ribosomes working on a single strand of mRNA.

23
Q

Protein synthesis takes place in the cytoplasm with which exception?

A

Mitochondrial protein synthesis.

24
Q

What is the name for the first 20-24 amino acids?

A

Signal sequence

25
Q

What does the signal sequence bind to?

A

Signal reception particle on ER

26
Q

What happens when a signal sequence is recognised by a SRP?

A

Translation halts, SS binds to SRP, translation resumes

Protein channel forms in ER, and protein enters.

27
Q

What happens when the preproprotein has entered the ER?

A

The signal sequence is cleaved by signal peptidase creating a proprotein.

28
Q

What will be present is the protein is destined to become a transmembrane protein?

A

Extra hydrophobic sequence at C terminus which integrates into membrane

29
Q

What allows the signal sequence to easily travel across membranes?

A

It is hydrophobic. (Lipophilic)

30
Q

Name the ways a proteins tertiary structure can be modified!

There are 6/7

A
Disulphide bond formation
Proteolytic cleavage
Glycosylation	(addition	of	carbohydrate)
Phosphorylation (addition of phosphate)
Prenylation, Acylation (addition of lipid groups)	
Hydroxylation