Interactions of the Escherichia coli hydrogenase biosynthetic proteins: HybG complex formation

FEBS Lett. 2006 Jan 23;580(2):677-81. doi: 10.1016/j.febslet.2005.12.063. Epub 2005 Dec 28.


Assembly of the active site of the [NiFe]-hydrogenase enzymes involves a multi-step pathway and the coordinated activity of many accessory proteins. To analyze complex formation between these factors in Escherichia coli, they were genomically tagged and native multi-protein complexes were isolated. This method validated multiple interactions reported in separate studies from several organisms and defined a new complex containing the putative chaperone HybG and the large subunit of hydrogenase 1 or 2. The complex also includes HypE and HypD, which interact with each other before joining the larger complex.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Escherichia coli / enzymology*
  • Escherichia coli Proteins / genetics
  • Escherichia coli Proteins / metabolism*
  • Gene Targeting
  • Hydrogenase / biosynthesis*
  • Molecular Chaperones / genetics
  • Molecular Chaperones / metabolism*
  • Multiprotein Complexes


  • Escherichia coli Proteins
  • HybG protein, E coli
  • Molecular Chaperones
  • Multiprotein Complexes
  • Hydrogenase