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Originally Posted by RobJim
Well, one of the basic ways that chaperonins work is to block other molecules from interacting with the folding protein. Some proteins have hydrophobic residues that might interact with similar hydrophobic residues on other proteins before the protein finishes folding. This causes aggregation of improperly folded proteins.
Did the 'first cell' have chaperonins? Possibly. In pre-biotic conditions there was almost certainly a complex evolutionary process occurring which acted on RNA and/or maybe other molecules. The existence of a full cell wasn't necessarily required for complex molecular interactions.
I am not familiar with chaperonins in general, but I'll look into it.
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Hi! Thanks!
I did little search and I think that I understand mechanism now but still I didn't find answers to most of my questions
What's their origin? And did "first cell" contain genes for them?What if there would be a mutation and and some chaperonin would be nonfunctional? Would it be lethal?
You said that the first cell probably contained genes for them and I agree cause I read that ribosomes in prokaryotes don't have chaperonins function so it would be lethal for prokaryotes not to have them or to have a fatal mutation but I'm not sure for eukaryotes cause their ribosomes have that function...
so does that mean that most of mutations in genes for chaperones wouldn't be lethal?
And I read that mutation for hsp90 would be lethal in early embrionic stage....
Now do you know some diseases related to non functional chaperones?
ps most informations from
http://www.chaperone.sote.hu/Examples.html
THANKS!
Jana