ER Flashcards

1
Q

Start of Endomembrane system

A

RER

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

Polypeptides are synthesized at two location

A

-1/3 at RER
-2/3 on free cytosolic ribosomes

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

Protein synthesized at RER

A
  • secreted proteins
  • transmembrane proteins
  • soluble proteins reside in Endomembrane system
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Protein synthesized on free cytosolic ribosomes

A

-proteins destined to remain in ribosomes
-peripheral proteins of cytosolic surfaces
-proteins transported to nucleus
-proteins for chloroplast/chloroplast/peroxisome

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

All proteins begin synthesis in

A

Ribosomes in cytosol

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

How proteins know where to go

A

ER signal sequence OR sorting signal

TIGHTLY TIE PROTEIN SEQUENCE,SYNTHESIS,TARGETING

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

Translation start at

A

Cytosol

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

Most polypeptide synthesis take place in

A

Cytosol

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

After translation two pathways separated

A

Free ribosome vs ER-docked ribosome

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

Protein sorting pathways

A

1- Co-translational import
2- post-translational import

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

Co and post translational import difference

A

Co:
Proteins carry ER signal sequence direct to RER
——ER signal sequence

Post:
Lack of ER signal sequence, complete synthesis on free ribosome
——sorting signal

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

The proteins are released in cytoplasm from post-translational import and ———

A

Those who have organelle-specific sorting signal are imported into organelle
**cytoplasmic proteins do not have sorting signal

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

Multiple ribosome synthesizing same mRNA

A

Polysome

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

Co translational translocation of SOLUBLE PROTEIN

A

Deposit polypeptides in lumen of ER

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

Signal Recognition Particle (SRP)

A

Binds ribosome-mRNA-polypeptide complex to ER membrane

SRP bind ER signal sequence to new forming polypeptide

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

SRP contain

A

Protein and RNA

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Polypeptide synthesis proceed until

A

ER signal sequence has been formed

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Srp bind to signal sequence and ———

A

Block further translations

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

ER signal sequence inserted into translocation once ———

A

SRP has been released

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

How the channel to ER lumen opens?

A

ER signal sequence contact interior of translocon

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

When polypeptide synthesis is complete

A
  • polypeptide released into lumen
  • ribosome detaches from ER membrane
    -translocon pore closes
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

G protein (GTPases)

A

Molecular switch between GTP- and GDP- bound state
Different conformations= different affinities

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

G-proteins play roles in

A
  • cell signaling
  • cell division
  • proteins synthesis
  • vesicle fusion
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

SRP and SRP are

A

Both G protein

25
One mahor group of polypeptide synthesized on RER is molecules destined to be
Integral Membrane Proteins
26
Transmembrane proteins can be
Single or multi pass
27
Oligosaccharide chains are always ———
On non-cytosolic side
28
Translocon and membrane have
Charge asymmetry —— more negative on cytosolic side
29
Hydrophobic transmembrane domain can ——— in lipid bilayer
Dissolve
30
Orientation of multi-pass protein integral membrane protein is determined by ———
Charge/orientation of first transmembrane domain —— each subsequent transmembrane domain must have opposite charge
31
RER is site of
-Protein modification -recognition and removal of misfolded proteins -lipid synthesis
32
Glycosylation in (ER and Golgi) =
Glycoproteins
33
Most proteins synthesized in RER are glycosylated on ———
amide nitrogen of asparagine
34
Glycosylation is then modified by
Golgi
35
Carbohydrate groups in glycoproteins function as :
-macromolecule binding site -aid protein folding -increase stability
36
Co-translational glycosylation
Oligosaccharides are added to protein during synthesis
37
Processing of the N-linked oligosaccharide in ER lumen
Initial process when 3 glucose residue and 1 mannose are removed WHY? Possible sort of signal indicating
38
As polypeptides enter ER lumen
Fold into final shape
39
Chaperones of N-linked oligosacvharides
Calnexin and calreticulin
40
Binding of calnexin and calreticulin ———
Prevent aggregation and drives disulfide bond formation
41
Bip
Binding proteins chaperone Binds to hydrophobic regions and prevent interactions
42
Bip release the polypeptide chain then:
If fold correctly, hydrophobic region is buried in the interior If fold incorrectly, interacts with BiP again
43
Disulfide bond formation enzyme
Protein disulfide isomerase PDI
44
In eukaryotic cells, disulfide bonds are only formed in
ER lumen
45
Disulfide bond formation occurs between
Adjacent cysteines
46
Proteins can be —— faster than they can be ——
Made faster than fold
47
Higher made than fold activate
Unfolded Protein Response (UPR)
48
UPR will
Sensor molecules in ER detect misfolded proteins
49
When UPR is activated
1- phosphorylate translation factor (Inhibiting protein synthesis) 2- upregulate the expression: — er based chaperones — transport proteins out of ER — protein degradation machinery
50
Component of UPR that recognize misfolded or unassembled proteins
ER-associated degradation (ERAD)
51
What happen to misfolded proteins
Export to cytosol and degraded by proteasomes
52
Proteasomes
Bind ubiquitin-labeled proteins Remove ubiquitin Fed the protein in central channel
53
Ubiquitin is joined to target protein by
3enzymes E1—— ubiquitin activating E2—— ubiquitin conjugating E3—— ubiquitin ligase
54
Primary source of membrane lipid
ER
55
Why ER is primary
Because other doesn’t have the required enzymes
56
Except ER who can produce lipid
Mitochondria, chloroplasts, peroxisomes
57
Fatty acids required for lipid synthesis
Are synthesized in cytoplasm then go to ER membrane on cytosolic side Then, transfer to lumenal side by flippases
58
Most organelles have enzymes modifying lipids
Converting one type to another
59
Exchange lipids between compartment
Lipid Transfer Protein