Protein Sorting and Trafficking Flashcards

0
Q

how are proteins destined for mitochondria transported?

A

By chaperone proteins in the unfolded state as only one a,ino acid fits through translocation channel.

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1
Q

In the ER what constitutes the signal sequence and how does it differ to that for the mitochondria, nucleus and lysosome?

A

9 hydrophobic amino acids.
3 Arg residues.
Basic +ve amino acids.
Mannose-6-phosphate tag.

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2
Q

what modifications are made to proteins in the ER and in the Golgi? What happens to incorrectly folded proteins?

A

disulphide bonds may form.
Sugars are added (increases ss diversity).
they don’t enter the Golgi

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3
Q

what are glycosyltransferases?

A

Golgi enzymes which add sugars to proteins on red blood cells giving blood groups.

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4
Q

what is a stop transfer sequence?

A

v. hydrophobic sequence of ~ 20-22 amino acids = length of a membrane - remain as TRANSMEMBRANE SEGMENTS.

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5
Q

where can the mannose 6 phosphate receptor be found and what does it do?

A

in the golgi

directs proteins into transport vesicles destined for lysosomes.

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