RNA-mediated chaperone type for de novo protein folding.

Abstract:

:Traditionally the principles of protein folding in vivo have been obtained largely from molecular chaperone studies. Through extensive studies on molecular chaperones, it becomes clear that most proteins can fold without their assistance in vivo, suggesting the existence of other chaperone types and mechanisms. Since all nascent polypeptides are linked to the ribosomes, protein folding in vivo should be understood in the context of vectorial protein synthesis and linkage of nascent chains to ribosome whose major components and basic structural frames are RNAs. Here we introduce a novel RNA-mediated chaperone type and a possible molecular basis for how RNAs can exert chaperoning effect on their linked aggregation-prone polypeptides. Extending potential chaperoning role of ribosome on the bound nascent polypeptide in a cis-acting manner, the findings further suggest a novel function of RNA molecules for protein folding inside cells. RNA interaction-mediated stabilization of folding intermediate against aggregation provides new insights into de novo protein folding in vivo and further extends the functional diversity of RNA molecules.

journal_name

RNA Biol

journal_title

RNA biology

authors

Choi SI,Ryu K,Seong BL

doi

10.4161/rna.6.1.7441

subject

Has Abstract

pub_date

2009-01-01 00:00:00

pages

21-4

issue

1

eissn

1547-6286

issn

1555-8584

pii

7441

journal_volume

6

pub_type

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