Session 9 no protein targeting yet!!(Protein Processing And Targeting) Flashcards

1
Q

Name the 2 types of processing

A
Proteolytic cleavage (breaking)
Covalent modification (adding groups)
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2
Q

What happens to proteins made on free ribosomes?

A

They stay in the cytosol/go into organelles

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3
Q

What happens to proteins made on RER ribosomes?

A

They go to the membrane or secretory pathways

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4
Q

What is needed for protein sorting?

A

Signalling sequence
Receptor
Translocation machinery
Energy

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5
Q

What do membrane proteins have within their sequences?

A

Stop-transfer anchor sequence

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6
Q

In terms of secretory proteins, what does SRP stand for?

A

Signal recognition particle

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7
Q

List the functions of the ER (7)

A
Assembly of multi subunit proteins 
Hydroxylation of selected Lys and Pro residue 
Glycosylation
Forms S-S bonds
Proper folding of proteins
Specific Proteolytic cleavage 
Insertion of proteins into membranes
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8
Q

What is used to protect nascent proteins?

A

Chaperone proteins (which can correct problems in structure)

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9
Q

What is glycosylation?

A

Adding a carbohydrate to a molecule

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10
Q

Describe the processing of production insulin from pre-proinsulin (3)

A

(Entering ER)- signal peptide cleaved - proinsulin
(In ER lumen)- disulphides bridges are formed -proinsulin
(In GA)- introns removed (B chain)- insulin

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