Quiz
ER Transport and Glycosylation
Questions in this quiz (20)
1Describe the structure of Sec61
- ATrimeric- Alpha, beta and gamma subunits
- BDimeric- 1A & 1B subunits
- CTetrameric- A, B, C & D subunits
2What of the role of Sec 61 in ER transport?
- AForms the pore itself
- BBinds the nascent polypeptide
- CFolds the nascent polypeptide once it's passed through
3Which pore-associated protein interacts with the signal recognition particle?
- ASR-alpha
- BSR-beta
- CSR-gamma
4What is the role of the Sec62/63 complex?
- AContains a J domain
- BContains a G/F domain
- CThat signals the ATPase domain of Hsp40 in the ER (Bip)
- DThat signals the ATPase domain of Hsp70 in the ER (Bip)
5The Bip protein acts as a ratchet, pulling the protein through and preventing it moving backwards
- ATrue
- BFalse
6The first Asparagine to enter the ER has what added to it?
- AMannose
- BAcetyl-N Glucosamine
- CAcetyl-N Galactosamine
- DMoiety
7The sugar added to the Asparagine is 12 residues long
- ATrue
- BFalse
8Once the sugar has been added, what happens?
- AGlucosidase 1 & 2 remove glucose residues
- BFructosidase 1 & 2 remove fructose residues
- CGalactosidase 1 & 2 remove galactose residues
9Once the residues have been removed, the protein is folded by one of which chaperones?
- ACalnexin
- BCalreticulin
- CCal-Chaperonin
- DCalregulin
10The Cal_ protein doing the folding will be bound to Erp57
- ATrue
- BFalse
11What happens after the protein has been folded?
- AAnother glucose is removed
- BAnother fructose is removed
- CAnother galactose is removed
12Once the final residue is removed, the protein enters ERAD quality control, in which 2 things can happen
- ATrue
- BFalse
13Other than exiting the ER as a correctly folded protein, what can happen after protein folding is complete?
- AProtein is reglycosylated
- BProtein has mannose residues removed
- CProtein has ions added
- DProtein is degraded
14In the case of a misfolding that the ER can correct, what protein is used to signal this?
- AGlycoprotein Glycosyl Transferase
- BMannosidase I
- CEDM's
15What proteins remove mannose resiudes of proteins to be degraded?
- AGlucosidase
- BGlycoprotein Glycosyl Transferase
- CMannosidase
- DEDM's
16Which protein leads a misfolded protein out of the ER to be degraded in the protesome?
- AHrd1-E3
- BGlycoprotein Glycosyl Transferase
- CSec53
- DYDJ1
17What is the role of Epr-57?
- ATo make/break disulphide bonds
- BTo cleave Signal Recognition Particle
- CTo bind Calreticulin to the membrane
18Calnexin is membrane bound, Calreticulin is not
- ATrue
- BFalse
19In Cal_ and Cal_, where on the protein to be folded to they bind?
- ALectin domain- an exposed glucose residue
- BPectin domain- an exposed Fructose residue
- CPlectrin domain- an exposed mannose residue
20The protein end not bound to the sugar residue binding site is bound to what?
- AThe membrane
- BErp-57
- CSSa
Information
- Description
- Structural Basis for Biological Function (Protein Translocation) Quiz on ER Transport and Glycosylation, created by gina_evans0312 on 21/12/2013.
- Author
- gina_evans0312
- Language
- English
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