Structural disorder throws new light on moonlighting.

TitleStructural disorder throws new light on moonlighting.
Publication TypeJournal Article
Year of Publication2005
AuthorsTompa, P., C. Szász, and L. Buday
JournalTrends Biochem Sci
Volume30
Issue9
Pagination484-9
Date Published2005 Sep
ISSN0968-0004
KeywordsBinding Sites, Down-Regulation, Protein Biosynthesis, Proteins, Structure-Activity Relationship, Up-Regulation
Abstract

A basic mechanism by which individual proteins can increase network complexity is moonlighting, whereby a given protein fulfils more than one function. Traditionally, this phenomenon is attributed to separate binding surfaces of globular, folded proteins but we suggest that intrinsically unstructured proteins (IUPs) might provide radically different mechanisms. Eleven IUPs have been identified that suggest that the structural malleability of IUPs gives rise to unprecedented cases of moonlighting by eliciting opposing (inhibiting and activating) action on different partners or even the same partner molecule. Unlike classical cases, these proteins use the same region or overlapping interaction surfaces to exert distinct effects and employ non-conventional mechanisms to switch function, enabled by their capacity to adopt different conformations upon binding. Owing to the apparent functional benefits, we expect to see many more examples of this parsimonious use of protein material in complex metabolic networks.

DOI10.1016/j.tibs.2005.07.008
Alternate JournalTrends Biochem. Sci.
PubMed ID16054818
Grant List / / Wellcome Trust / United Kingdom