ER Transport and Glycosylation

Descrição

Structural Basis for Biological Function (Protein Translocation) Quiz sobre ER Transport and Glycosylation, criado por gina_evans0312 em 21-12-2013.
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Quiz por gina_evans0312, atualizado more than 1 year ago
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Criado por gina_evans0312 mais de 10 anos atrás
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Resumo de Recurso

Questão 1

Questão
Describe the structure of Sec61
Responda
  • Trimeric- Alpha, beta and gamma subunits
  • Dimeric- 1A & 1B subunits
  • Tetrameric- A, B, C & D subunits

Questão 2

Questão
What of the role of Sec 61 in ER transport?
Responda
  • Forms the pore itself
  • Binds the nascent polypeptide
  • Folds the nascent polypeptide once it's passed through

Questão 3

Questão
Which pore-associated protein interacts with the signal recognition particle?
Responda
  • SR-alpha
  • SR-beta
  • SR-gamma

Questão 4

Questão
What is the role of the Sec62/63 complex?
Responda
  • Contains a J domain
  • Contains a G/F domain
  • That signals the ATPase domain of Hsp40 in the ER (Bip)
  • That signals the ATPase domain of Hsp70 in the ER (Bip)

Questão 5

Questão
The Bip protein acts as a ratchet, pulling the protein through and preventing it moving backwards
Responda
  • True
  • False

Questão 6

Questão
The first Asparagine to enter the ER has what added to it?
Responda
  • Mannose
  • Acetyl-N Glucosamine
  • Acetyl-N Galactosamine
  • Moiety

Questão 7

Questão
The sugar added to the Asparagine is 12 residues long
Responda
  • True
  • False

Questão 8

Questão
Once the sugar has been added, what happens?
Responda
  • Glucosidase 1 & 2 remove glucose residues
  • Fructosidase 1 & 2 remove fructose residues
  • Galactosidase 1 & 2 remove galactose residues

Questão 9

Questão
Once the residues have been removed, the protein is folded by one of which chaperones?
Responda
  • Calnexin
  • Calreticulin
  • Cal-Chaperonin
  • Calregulin

Questão 10

Questão
The Cal_ protein doing the folding will be bound to Erp57
Responda
  • True
  • False

Questão 11

Questão
What happens after the protein has been folded?
Responda
  • Another glucose is removed
  • Another fructose is removed
  • Another galactose is removed

Questão 12

Questão
Once the final residue is removed, the protein enters ERAD quality control, in which 2 things can happen
Responda
  • True
  • False

Questão 13

Questão
Other than exiting the ER as a correctly folded protein, what can happen after protein folding is complete?
Responda
  • Protein is reglycosylated
  • Protein has mannose residues removed
  • Protein has ions added
  • Protein is degraded

Questão 14

Questão
In the case of a misfolding that the ER can correct, what protein is used to signal this?
Responda
  • Glycoprotein Glycosyl Transferase
  • Mannosidase I
  • EDM's

Questão 15

Questão
What proteins remove mannose resiudes of proteins to be degraded?
Responda
  • Glucosidase
  • Glycoprotein Glycosyl Transferase
  • Mannosidase
  • EDM's

Questão 16

Questão
Which protein leads a misfolded protein out of the ER to be degraded in the protesome?
Responda
  • Hrd1-E3
  • Glycoprotein Glycosyl Transferase
  • Sec53
  • YDJ1

Questão 17

Questão
What is the role of Epr-57?
Responda
  • To make/break disulphide bonds
  • To cleave Signal Recognition Particle
  • To bind Calreticulin to the membrane

Questão 18

Questão
Calnexin is membrane bound, Calreticulin is not
Responda
  • True
  • False

Questão 19

Questão
In Cal_ and Cal_, where on the protein to be folded to they bind?
Responda
  • Lectin domain- an exposed glucose residue
  • Pectin domain- an exposed Fructose residue
  • Plectrin domain- an exposed mannose residue

Questão 20

Questão
The protein end not bound to the sugar residue binding site is bound to what?
Responda
  • The membrane
  • Erp-57
  • SSa

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