4.4 Article

Repurposing TRASH: Emergence of the enzyme organomercurial lyase from a non-catalytic zinc finger scaffold

Journal

JOURNAL OF STRUCTURAL BIOLOGY
Volume 188, Issue 1, Pages 16-21

Publisher

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jsb.2014.09.001

Keywords

MerA; MerH; NosL; Domain duplication; Domain fusion; Promiscuous enzymes; Enzyme evolution

Funding

  1. Council of Scientific and Industrial Research (CSIR)-Institute of Microbial Technology, Chandigarh, India
  2. XII five-year plan network project, Biodiscovery [BSC0120K]
  3. CSIR, India

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The mercury resistance pathway enzyme organomercurial lyase (MerB) catalyzes the conversion of organomercurials to ionic mercury (Hg2+). Here, we provide evidence for the emergence of this enzyme from a TRASH-like, non-enzymatic, treble-clef zinc finger ancestor by domain duplication and fusion. Surprisingly, the structure-stabilizing metal-binding core of the treble-clef appears to have been repurposed in evolution to serve a catalytic role. Novel enzymatic functions are believed to have evolved from ancestral generalist catalytic scaffolds or from already specialized enzymes with catalytic promiscuity. The emergence of MerB from a zinc finger ancestor serves as a rare example of how a novel enzyme may emerge from a non-catalytic scaffold with a related binding function. (C) 2014 Elsevier Inc. All rights reserved.

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