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Structural Basis for Biological Function (Protein Translocation) Quiz on ER Transport and Glycosylation, created by gina_evans0312 on 12/21/2013.

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ER Transport and Glycosylation

ER Transport and Glycosylation

Question 1 of 20

1

Describe the structure of Sec61

Select one of the following:

  • Trimeric- Alpha, beta and gamma subunits

  • Dimeric- 1A & 1B subunits

  • Tetrameric- A, B, C & D subunits

Explanation

Question 2 of 20

1

What of the role of Sec 61 in ER transport?

Select one of the following:

  • Forms the pore itself

  • Binds the nascent polypeptide

  • Folds the nascent polypeptide once it's passed through

Explanation

Question 3 of 20

1

Which pore-associated protein interacts with the signal recognition particle?

Select one of the following:

  • SR-alpha

  • SR-beta

  • SR-gamma

Explanation

Question 4 of 20

1

What is the role of the Sec62/63 complex?

Select one or more of the following:

  • 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)

Explanation

Question 5 of 20

1

The Bip protein acts as a ratchet, pulling the protein through and preventing it moving backwards

Select one of the following:

  • True
  • False

Explanation

Question 6 of 20

1

The first Asparagine to enter the ER has what added to it?

Select one of the following:

  • Mannose

  • Acetyl-N Glucosamine

  • Acetyl-N Galactosamine

  • Moiety

Explanation

Question 7 of 20

1

The sugar added to the Asparagine is 12 residues long

Select one of the following:

  • True
  • False

Explanation

Question 8 of 20

1

Once the sugar has been added, what happens?

Select one of the following:

  • Glucosidase 1 & 2 remove glucose residues

  • Fructosidase 1 & 2 remove fructose residues

  • Galactosidase 1 & 2 remove galactose residues

Explanation

Question 9 of 20

1

Once the residues have been removed, the protein is folded by one of which chaperones?

Select one or more of the following:

  • Calnexin

  • Calreticulin

  • Cal-Chaperonin

  • Calregulin

Explanation

Question 10 of 20

1

The Cal_ protein doing the folding will be bound to Erp57

Select one of the following:

  • True
  • False

Explanation

Question 11 of 20

1

What happens after the protein has been folded?

Select one of the following:

  • Another glucose is removed

  • Another fructose is removed

  • Another galactose is removed

Explanation

Question 12 of 20

1

Once the final residue is removed, the protein enters ERAD quality control, in which 2 things can happen

Select one of the following:

  • True
  • False

Explanation

Question 13 of 20

1

Other than exiting the ER as a correctly folded protein, what can happen after protein folding is complete?

Select one or more of the following:

  • Protein is reglycosylated

  • Protein has mannose residues removed

  • Protein has ions added

  • Protein is degraded

Explanation

Question 14 of 20

1

In the case of a misfolding that the ER can correct, what protein is used to signal this?

Select one of the following:

  • Glycoprotein Glycosyl Transferase

  • Mannosidase I

  • EDM's

Explanation

Question 15 of 20

1

What proteins remove mannose resiudes of proteins to be degraded?

Select one or more of the following:

  • Glucosidase

  • Glycoprotein Glycosyl Transferase

  • Mannosidase

  • EDM's

Explanation

Question 16 of 20

1

Which protein leads a misfolded protein out of the ER to be degraded in the protesome?

Select one of the following:

  • Hrd1-E3

  • Glycoprotein Glycosyl Transferase

  • Sec53

  • YDJ1

Explanation

Question 17 of 20

1

What is the role of Epr-57?

Select one of the following:

  • To make/break disulphide bonds

  • To cleave Signal Recognition Particle

  • To bind Calreticulin to the membrane

Explanation

Question 18 of 20

1

Calnexin is membrane bound, Calreticulin is not

Select one of the following:

  • True
  • False

Explanation

Question 19 of 20

1

In Cal_ and Cal_, where on the protein to be folded to they bind?

Select one of the following:

  • Lectin domain- an exposed glucose residue

  • Pectin domain- an exposed Fructose residue

  • Plectrin domain- an exposed mannose residue

Explanation

Question 20 of 20

1

The protein end not bound to the sugar residue binding site is bound to what?

Select one of the following:

  • The membrane

  • Erp-57

  • SSa

Explanation

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