Assisted Folding - Proteostasis

Question 1

what molecule assist the folding of proteins?

Answer 1

chaperone and chaperonins

Question 2

what are chaperones?

Answer 2

these are molecules that bind natively folding proteins and help with co-translational folding. They also prevent the aggregation of proteins that form oligomers, amourphous aggregates and eventually amyloid fibrils that cause disease.

Question 3

What about a cell’s intracellular environment warrants the need for chaperones

Answer 3

a cell can become very crowded with proteins being formed and folding.

Question 4

What is a chaperonin

Answer 4

these are barrel-like proteins that unfold misfiled proteins and allow the proteins to be corrected inside the barrel or get rid of protein that cannot be corrected.

Question 5

What happens when the protein folding cannot be corrected?

Answer 5

The misfolded protein is tagged for upiquitination. After being polyunbiquinated the protein is sent to a proteasome that breaks it down into its peptides that can be recycled.

Question 6

What is the purpose of these chaperonins and chaperones?

Answer 6

These molecules maintain proteostatis or the normal folding of proteins.

Question 7

What disease can deficiencies in proteostasi cause?

Answer 7

1. neurodegeneration
2. type 11 diabetes
3. peripheral amyloidosis
4. lysosomal storage disease
5. cystic fibrosis
6. cancer
7. cardiovascular disease