Intrinsically disordered chaperones in plants and animals.

TitleIntrinsically disordered chaperones in plants and animals.
Publication TypeJournal Article
Year of Publication2010
AuthorsTompa, P., and D. Kovacs
JournalBiochem Cell Biol
Volume88
Issue2
Pagination167-74
Date Published2010 Apr
Type of Articleidp
ISSN1208-6002
KeywordsAnimals, Chaperonins, Plants, Protein Folding
Abstract

Intrinsically disordered proteins (IDPs) are widespread in eukaryotes and fulfill important functions associated with signaling and regulation. Recent evidence points to a special and thus largely disrespected functional capacity of IDPs--that they can assist the folding of other proteins and prevent their aggregation, i.e., that they can act as chaperones. In this paper, we survey current information available on this phenomenon, with particular focus on (i) the structure and function of IDPs in general, (ii) disordered chaperones in plants, (iii) disordered chaperones in other organisms spanning from insects to mammals, (iv) the possible mechanisms of action of disordered chaperones, and (v) the possibility of two-faced (Janus) chaperone activity of disordered chaperones, which can assist the folding of both RNA and protein substrates. The evidence is most conclusive in the case of plant stress proteins, such as late embryogenesis abundant (LEA) proteins or dehydrins. We will show that the cellular function of LEA proteins in mitigating the damage caused by stress is clear; nevertheless, experiments carried out in vivo must be extended and the molecular mechanism of the action of IDP chaperones also requires clarification. Using these details, we chart out how far the field has progressed only to emphasize the long road ahead before chaperone function can be firmly established as part of the physiological mechanistic arsenal of the emerging group of IDPs.

DOI10.1139/o09-163
Alternate JournalBiochem. Cell Biol.
PubMed ID20453919