MCGB - Protein Processing And Targeting - done to slide 21 Flashcards Preview

CJ: UoL Medicine Semester One (ESA1) > MCGB - Protein Processing And Targeting - done to slide 21 > Flashcards

Flashcards in MCGB - Protein Processing And Targeting - done to slide 21 Deck (36)
Loading flashcards...
1
Q

If proteases were activated while they are still inside the cell they were synthesised in, they would destroy the cell. How is this issue overcome?

A

They are activated outside the cell in “post-translational modification.”

2
Q

What is proteolytic cleavage?

A

Breaking peptide bonds to remove part of the protein.

3
Q

What is chemical modification?

A

The addition of functional groups to amino acid residues.

4
Q

If a protein is destined for the cytosol or for posttranslational import into organelles, where is it synthesised?

A

Free ribosomes

5
Q

If a protein is destined for the membrane, lysosomes, secretory vesicles or other organelles, where is it synthesised?

A

Ribosomes on rough ER.

6
Q

What is required for protein sorting?

A

A SIGNAL intrinsic to the protein, a RECEPTOR which can recognise the signal and direct it to the correct membrane, a TRANSLOCATION machinery, ENERGY to transfer protein to new place.

7
Q

Which type of protein targeting is this? Three amino acids termed the “PTS” are present on the C-terminus of the protein. PTS is recognised by PTS receptor Pex5 which binds to “cargo protein”, 13 Pex proteins make up a transport channel across membrane of organelle, binds to Pex5-cargo complex. ATP hydrolysis required for recycling of receptor.

A

Protein targeting to peroxisomes

8
Q

What is the difference between constitutive and regulated secretion?

A

Constitutive - going on all the time, constant flow of extracellular proteins out of the cell, eg. Fibroblasts

Regulated - occurs at specific times from cell, eg. Neurocrine cells

9
Q

Give some characteristics of a signal sequence of a secreted protein.

A

N-terminal amino acid sequence, 5-30 amino acids in length, central region rich in hydrophobic residues, able to form alpha helix.

10
Q

What is post translational modification?

A

The changes made to proteins after they are formed.

11
Q

Give some examples of proteins that would be targeted for secretion.

A

Extracellular proteins, membrane proteins, vesicular proteins eg lysosomes.

12
Q

Ina cell that secretes proteins there is a lot of one particular organelle. Which one?

A

RER

13
Q

Why is it important that secreted proteins are able to form an alpha helix?

A

It allows them to quickly cross the lipid bilayer.

14
Q

What is a signal recognition particle?

A

A molecule composed of six proteins and a short piece of RNA which recognises the signal peptide and the ribosome.

15
Q

Give some functions of the endoplasmic reticulum.

A

Insertion of proteins into membranes, specific proteolytic cleavage, glycosylation, formation of disulphide bonds, proper folding/assembly of proteins, hydroxylation of residues.

16
Q

What is N-linked glycosylation?

A

Adding a sugar group to an amino acid through a nitrogen group in the ER.

17
Q

Why is glycosylation of proteins important?

A

Provides stability, facilitates interaction with other molecules, allows correct protein folding.

18
Q

What is the role of protein disulphide isomerase?

A

It ensures the correct disulphide bond forms and replaces them if incorrect.

19
Q

Why is it less of an issue if protein misfolding occurs in the ER?

A

ER chaperone proteins can help the protein to refold correctly.

20
Q

What happens to a mis-folded protein which cannot be corrected?

A

It is returned to the cytosol for degradation.

21
Q

What is O-linked glycosylation?

A

Attachment of a sugar to an OH group, which occurs in the Golgi complex.

22
Q

Collagen is not very abundant in the body - true or false?

A

False, it’s the most abundant.

23
Q

What is a collagen fibre made up of?

A

Molecules called TROPOCOLLAGEN (rod shaped protein, made of 3 polypeptides, repeated glycine structure, triple helix)

24
Q

Give some characteristics of the triple helix structure of collagen.

A

Non-extensible, non-compressible, high tensile strength.

25
Q

Why is glycine present in every third position of the alpha helix of collagen?

A

Glycine is the only amino acid small enough to fit into the middle of the helix.

26
Q

What sort of bonds form between alpha chains to stabilise the structure?

A

Hydrogen bonds.

27
Q

Which organelle do fibroblasts have an uncommonly large amount of?

A

RER

28
Q

The signal peptide is cleaved off as the prepro alpha chains of collagen enter the ER. What are they then called?

A

Pro alpha chains

29
Q

Why are collagen molecules weaker if sufficient vitamin C is not present?

A

The amino acids cannot be hydroxylated, so they cannot form hydrogen bonds and the molecule is weaker (scurvy).

30
Q

Outline the stages of tropocollagen formation and modification.

A

1) synthesis and entry to lumen of RER
2) cleavage of signal peptide
3) hydroxylation of Pro and Lys
4) N-glycosylation and galactose added
5) chain alignment, S-S bonds
6) precollagen forms
7) glucose added, enters transport vesicle
8) exocytosis, removal of N and C terminal propeptides

31
Q

What is removed when procollagen is transformed into tropocollagen?

A

N and C terminal peptides

32
Q

How does tropocollagen form collagen?

A

N and C terminal propeptides removed, collagen molecules laterally associated and covalently cross-linked, aggregation of fibrils.

33
Q

What does lysyl oxidise cause tropocollagens to do?

A

Form cross-links

34
Q

Why must tropocollagen be secreted outside the cell?

A

It is extremely large when cross-linked and would destroy the cell if it formed inside.

35
Q

Give some examples of disorders that can occur if targeting to peroxisomes goes wrong.

A

Zellweger syndrome, Rhizomelic Chondrodysplasia Punctata (both are peroxisome biogenesis disorders)

36
Q

What is a signal sequence?

A

N-terminal sequence of 5-30 amino acids

Decks in CJ: UoL Medicine Semester One (ESA1) Class (55):