Protein processing Flashcards

You may prefer our related Brainscape-certified flashcards:
1
Q

What is protein sorting?

A

It is how proteins know where to go in the cell

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Where is regulated secretion seen?

A

In the endocrine, exocrine and neurocrine systems

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

If ribosomes attach to the ER membrane, where is the protein destined for?

A

The cell membrane or a secretory pathway via co-translational insertion

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Ribosomes remain cystolic if….

A

The protein is destined for the cytosol, or post-translational import into organelles

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

What are the four requirements for protein sorting?

A
  • Intrinsic signal in the protein
  • Specific receptors to recognise the signal
  • Translation machinery
  • Energy to transfer the protein to its new place
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

At which terminus are signal sequences found in secretory proteins?

A

The N-terminus

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Which enzyme in the ER assists with forming disulphide bonds?

A

Protein disulphide isomerase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

N-linked glycosylation takes place in which organelle? And to which amino acid are sugars added?

A

It takes place in the ER. Sugars are added to a asparagine side chain

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

What is the function of peptidyl-propyl isomerases?

A

It is there function to accelerate the interconversion of cis- and tran- isomers of proline residues. This greatly facilitates rapid protein folding.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What is O-linked glycosylation?

A

It is the modification of the hydroxyl groups on serine and threonine. Glycosyl transferase builds up a sugar chain from nucleotide sugar substrates. This takes place in the Golgi

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

What enzyme catalyses the hydroxylation of proline and lysine residues in collagen?

A

Propyl hydroxylase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

What is added to the hydroxylysine residues of collagen?

A

Galactose

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Where does the synthesis and modification of collagen take place?

A

In the rough ER

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Tropocollagen is made of?

A

3 alpha chains

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

The conversion of …. to …. occurs extracellularly via procollagen peptidases

A

Procollagen to tropocollagen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Cross linking occurs between lysine residues on the tropocollagen. It is catalysed by which enzyme? A mutation to this enzyme results in which condition?

A

Lysyl oxidase. A mutation results in Ehler-Danlos

17
Q

Proinsulin undergoes disulphide bond formation in the……

A

Endoplasmic reticulum

18
Q

Where does protein processing of proinsulin occur?

A

The Golgi

19
Q

What is the nature of the signal for retention within the ER?

A

K-D-E-L

20
Q

Where is the location of the signal within in the primary sequence if the protein is destined for the nucleus?

A

Various positions however it must be on the surface of folded proteins

21
Q

If the protein is destined for …. , …… and …… The signal is cleaved.

A

If the signal is to the ER, to the mitochondria or the lysosomes it is cleaved

22
Q

Which destination requires no energy in protein sorting?

A

Retention in the ER

23
Q

What is the name of the specialist protein involved in proteins sorted to the lysosomes?

A

M-6-P receptor