Selenate reductase activity in Escherichia coli requires Isc iron-sulfur cluster biosynthesis genes

FEMS Microbiol Lett. 2014 Dec;361(2):138-43. doi: 10.1111/1574-6968.12623. Epub 2014 Oct 31.

Abstract

The selenate reductase in Escherichia coli is a multi-subunit enzyme predicted to bind Fe-S clusters. In this study, we examined the iron-sulfur cluster biosynthesis genes that are required for selenate reductase activity. Mutants devoid of either the iscU or hscB gene in the Isc iron-sulfur cluster biosynthesis pathway lost the ability to reduce selenate. Genetic complementation by the wild-type sequences restored selenate reductase activity. The results indicate the Isc biosynthetic system plays a key role in selenate reductase Fe-S cofactor assembly and is essential for enzyme activity.

Keywords: Enterobacter; FNR; Salmonella; Suf; TAT; molybdoenzyme.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Biosynthetic Pathways
  • Escherichia coli / enzymology*
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Escherichia coli Proteins / genetics
  • Escherichia coli Proteins / metabolism
  • Heat-Shock Proteins / genetics
  • Heat-Shock Proteins / metabolism
  • Iron / metabolism*
  • Iron-Sulfur Proteins / genetics
  • Iron-Sulfur Proteins / metabolism
  • Multigene Family
  • Oxidation-Reduction
  • Oxidoreductases / genetics
  • Oxidoreductases / metabolism*
  • Selenic Acid / metabolism
  • Sulfur / metabolism*

Substances

  • Escherichia coli Proteins
  • Heat-Shock Proteins
  • HscB protein, E coli
  • Iron-Sulfur Proteins
  • IscU protein, E coli
  • Sulfur
  • Iron
  • Oxidoreductases
  • selenate reductase
  • Selenic Acid