451716
Description
Quiz by gina_evans0312, updated more than 1 year ago
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Created by gina_evans0312
over 10 years ago
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Question 1
Question
Describe the structure of Sec61
Answer
-
Trimeric- Alpha, beta and gamma subunits
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Dimeric- 1A & 1B subunits
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Tetrameric- A, B, C & D subunits
Question 2
Question
What of the role of Sec 61 in ER transport?
Answer
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Forms the pore itself
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Binds the nascent polypeptide
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Folds the nascent polypeptide once it's passed through
Question 3
Question
Which pore-associated protein interacts with the signal recognition particle?
Answer
-
SR-alpha
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SR-beta
-
SR-gamma
Question 4
Question
What is the role of the Sec62/63 complex?
Answer
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Contains a J domain
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Contains a G/F domain
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That signals the ATPase domain of Hsp40 in the ER (Bip)
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That signals the ATPase domain of Hsp70 in the ER (Bip)
Question 5
Question
The Bip protein acts as a ratchet, pulling the protein through and preventing it moving backwards
Answer
- True
- False
Question 6
Question
The first Asparagine to enter the ER has what added to it?
Answer
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Mannose
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Acetyl-N Glucosamine
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Acetyl-N Galactosamine
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Moiety
Question 7
Question
The sugar added to the Asparagine is 12 residues long
Answer
- True
- False
Question 8
Question
Once the sugar has been added, what happens?
Answer
-
Glucosidase 1 & 2 remove glucose residues
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Fructosidase 1 & 2 remove fructose residues
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Galactosidase 1 & 2 remove galactose residues
Question 9
Question
Once the residues have been removed, the protein is folded by one of which chaperones?
Answer
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Calnexin
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Calreticulin
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Cal-Chaperonin
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Calregulin
Question 10
Question
The Cal_ protein doing the folding will be bound to Erp57
Answer
- True
- False
Question 11
Question
What happens after the protein has been folded?
Answer
-
Another glucose is removed
-
Another fructose is removed
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Another galactose is removed
Question 12
Question
Once the final residue is removed, the protein enters ERAD quality control, in which 2 things can happen
Answer
- True
- False
Question 13
Question
Other than exiting the ER as a correctly folded protein, what can happen after protein folding is complete?
Answer
-
Protein is reglycosylated
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Protein has mannose residues removed
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Protein has ions added
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Protein is degraded
Question 14
Question
In the case of a misfolding that the ER can correct, what protein is used to signal this?
Answer
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Glycoprotein Glycosyl Transferase
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Mannosidase I
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EDM's
Question 15
Question
What proteins remove mannose resiudes of proteins to be degraded?
Answer
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Glucosidase
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Glycoprotein Glycosyl Transferase
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Mannosidase
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EDM's
Question 16
Question
Which protein leads a misfolded protein out of the ER to be degraded in the protesome?
Answer
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Hrd1-E3
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Glycoprotein Glycosyl Transferase
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Sec53
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YDJ1
Question 17
Question
What is the role of Epr-57?
Answer
-
To make/break disulphide bonds
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To cleave Signal Recognition Particle
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To bind Calreticulin to the membrane
Question 18
Question
Calnexin is membrane bound, Calreticulin is not
Answer
- True
- False
Question 19
Question
In Cal_ and Cal_, where on the protein to be folded to they bind?
Answer
-
Lectin domain- an exposed glucose residue
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Pectin domain- an exposed Fructose residue
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Plectrin domain- an exposed mannose residue
Question 20
Question
The protein end not bound to the sugar residue binding site is bound to what?
Answer
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The membrane
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Erp-57
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SSa
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