Structural disorder throws new light on moonlighting

Peter Tompa, Csilla Szász, László Buday

Research output: Contribution to journalArticle

368 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)484-489
Number of pages6
JournalTrends in Biochemical Sciences
Volume30
Issue number9
DOIs
Publication statusPublished - Sep 2005

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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