ER Transport and Glycosylation

1

Describe the structure of Sec61

1

What of the role of Sec 61 in ER transport?

1

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

1

What is the role of the Sec62/63 complex?

1

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

1

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

1

The sugar added to the Asparagine is 12 residues long

1

Once the sugar has been added, what happens?

1

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

1

The Cal_ protein doing the folding will be bound to Erp57

1

What happens after the protein has been folded?

1

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

1

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

1

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

1

What proteins remove mannose resiudes of proteins to be degraded?

1

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

1

What is the role of Epr-57?

1

Calnexin is membrane bound, Calreticulin is not

1

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

1

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

Structural Basis for Biological Function (Protein Translocation) Quiz am ER Transport and Glycosylation, erstellt von gina_evans0312 am 21/12/2013.

ER Transport and Glycosylation

Describe the structure of Sec61

What of the role of Sec 61 in ER transport?

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

What is the role of the Sec62/63 complex?

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

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

The sugar added to the Asparagine is 12 residues long

Once the sugar has been added, what happens?

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

The Cal_ protein doing the folding will be bound to Erp57

What happens after the protein has been folded?

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

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

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

What proteins remove mannose resiudes of proteins to be degraded?

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

What is the role of Epr-57?

Calnexin is membrane bound, Calreticulin is not

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

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