Interactions of the Escherichia coli hydrogenase biosynthetic proteins: HybG complex formation.
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.
Butland
Gareth
G
Banting and Best Department of Medical Research, University of Toronto, Toronto, Ont., Canada M5G 1L6.
Zhang
Jie Wei
JW
Yang
Wenhong
W
Sheung
Anthony
A
Wong
Peter
P
Greenblatt
Jack F
JF
Emili
Andrew
A
Zamble
Deborah B
DB
D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism*; D018390:Gene Targeting; D006864:Hydrogenase / Q000096:biosynthesis*; D018832:Molecular Chaperones / Q000235:genetics / Q000378:metabolism*; D046912:Multiprotein Complexes
D029968:Escherichia coli Proteins; C508780:HybG protein, E coli; D018832:Molecular Chaperones; D046912:Multiprotein Complexes; D006864:Hydrogenase