Secretion system- protein translocation Flashcards

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

What gram bacteria used the sec system

A

gram +ive and -ive

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

What is the purpose of sec system

A

insert protein in PM or transfer unfolded protein across PM

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

In which direction are proteins synthesized

A

in the N to C direction

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

describe the N and C terminus of proteins

A

has an unbound amino group and unbound carboxyl group respectively

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

What does it mean when an amino group is unbound

A

not convalently linked to the next one

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What are other names for the signal peptide

A

leader peptide or signal sequence

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

What are proteins w/a signal peptide called

A

preproteins

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

what is the hydrophobicity of the central part of the signal peptide

A

hydrophobic

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

Describe the signal peptide

A

proteins translocated by system are synthesized w/25 aa long peptide on N terminal

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

what is SecB

A

cytoplasmic chaperone (helper)

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

what is SecYEG

A

3 proteins that form an integral PM protein chain or translocase

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

What is secA

A

bound to inner surface of SecYEG, an ATPase meaning it hydrolyzes ATP

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

Where is the signal peptidase located

A

outer surface of PM

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

What is the fn of signal peptidase

A

removes the signal peptide from preprotein

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

How does secB, the chaperone protein have time to bind

A

as preprotein is being synthesized signal peptide slows folding of preprotein

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

What happeds after secB binds to preprotein

A

inhibits further folding and delivers preprotein to secA, secB is released

17
Q

How is the signal peptide inserted into the lipid bilayer

A

N terminius of signal peptide binds to surface of PM and hydrophobic region is inserted into bilayer. remainder of preprotein passes through a pore in SecYEG, at this point most is still in cytoplasm

18
Q

how is the preprotein released

A

secA hydrolyzes ATP

19
Q

how is the rest of the protein translocased to the periplasm

A

secYEG translocase uses PMF as nrg

20
Q

How is the signal peptide and protein separated

A

signal peptidase cuts signal peptidase, protein release into periplasm and folds into its tertiary structure