451716
Descripción
Test por gina_evans0312, actualizado hace más de 1 año
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Creado por gina_evans0312
hace casi 11 años
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Pregunta 1
Pregunta
Describe the structure of Sec61
Respuesta
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Trimeric- Alpha, beta and gamma subunits
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Dimeric- 1A & 1B subunits
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Tetrameric- A, B, C & D subunits
Pregunta 2
Pregunta
What of the role of Sec 61 in ER transport?
Respuesta
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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
Pregunta 3
Pregunta
Which pore-associated protein interacts with the signal recognition particle?
Respuesta
-
SR-alpha
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SR-beta
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SR-gamma
Pregunta 4
Pregunta
What is the role of the Sec62/63 complex?
Respuesta
-
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)
Pregunta 5
Pregunta
The Bip protein acts as a ratchet, pulling the protein through and preventing it moving backwards
Respuesta
- True
- False
Pregunta 6
Pregunta
The first Asparagine to enter the ER has what added to it?
Respuesta
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Mannose
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Acetyl-N Glucosamine
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Acetyl-N Galactosamine
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Moiety
Pregunta 7
Pregunta
The sugar added to the Asparagine is 12 residues long
Respuesta
- True
- False
Pregunta 8
Pregunta
Once the sugar has been added, what happens?
Respuesta
-
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
Pregunta 9
Pregunta
Once the residues have been removed, the protein is folded by one of which chaperones?
Respuesta
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Calnexin
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Calreticulin
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Cal-Chaperonin
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Calregulin
Pregunta 10
Pregunta
The Cal_ protein doing the folding will be bound to Erp57
Respuesta
- True
- False
Pregunta 11
Pregunta
What happens after the protein has been folded?
Respuesta
-
Another glucose is removed
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Another fructose is removed
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Another galactose is removed
Pregunta 12
Pregunta
Once the final residue is removed, the protein enters ERAD quality control, in which 2 things can happen
Respuesta
- True
- False
Pregunta 13
Pregunta
Other than exiting the ER as a correctly folded protein, what can happen after protein folding is complete?
Respuesta
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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
Pregunta 14
Pregunta
In the case of a misfolding that the ER can correct, what protein is used to signal this?
Respuesta
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Glycoprotein Glycosyl Transferase
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Mannosidase I
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EDM's
Pregunta 15
Pregunta
What proteins remove mannose resiudes of proteins to be degraded?
Respuesta
-
Glucosidase
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Glycoprotein Glycosyl Transferase
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Mannosidase
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EDM's
Pregunta 16
Pregunta
Which protein leads a misfolded protein out of the ER to be degraded in the protesome?
Respuesta
-
Hrd1-E3
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Glycoprotein Glycosyl Transferase
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Sec53
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YDJ1
Pregunta 17
Pregunta
What is the role of Epr-57?
Respuesta
-
To make/break disulphide bonds
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To cleave Signal Recognition Particle
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To bind Calreticulin to the membrane
Pregunta 18
Pregunta
Calnexin is membrane bound, Calreticulin is not
Respuesta
- True
- False
Pregunta 19
Pregunta
In Cal_ and Cal_, where on the protein to be folded to they bind?
Respuesta
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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
Pregunta 20
Pregunta
The protein end not bound to the sugar residue binding site is bound to what?
Respuesta
-
The membrane
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Erp-57
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SSa
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