title: The Escherichia coli metal-binding chaperone SlyD interacts with the large subunit of [NiFe]-hydrogenase 3.
abstract: The multi-step biosynthesis of the [NiFe]-hydrogenase enzyme involves a variety of accessory proteins. To further understand this process, a Strep-tag II variant of the large subunit of Escherichia coli hydrogenase 3, HycE, was constructed to enable isolation of protein complexes. A complex with SlyD, a chaperone protein implicated in hydrogenase production through association with the nickel-binding accessory protein HypB, was observed. A SlyD-HycE interaction preceding both iron and nickel insertion to the enzyme was detected, mediated by the chaperone domain of SlyD, and independent of HypB. These results support a model of several roles for SlyD during hydrogenase maturation.
authors.affiliation: Department of Chemistry, University of Toronto, Toronto, ON, Canada.
authors.forename: Kim C Chan
authors.initials: KC
authors.lastname: Chung
authors.forename: Deborah B
authors.initials: DB
authors.lastname: Zamble
mesh_terms: D002352:Carrier Proteins / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000378:metabolism*; D019204:GTP-Binding Proteins / Q000378:metabolism; D006864:Hydrogenase / Q000096:biosynthesis / Q000378:metabolism*; D047908:Intracellular Signaling Peptides and Proteins; D008670:Metals / Q000378:metabolism*; D046912:Multiprotein Complexes / Q000737:chemistry; D019696:Peptidylprolyl Isomerase / Q000378:metabolism*; D011485:Protein Binding
chemical_list: D002352:Carrier Proteins; D029968:Escherichia coli Proteins; C499625:HypA protein, E coli; C490324:HypB protein, E coli; D047908:Intracellular Signaling Peptides and Proteins; D008670:Metals; D046912:Multiprotein Complexes; C085606:SlyD protein, E coli; C086230:hycE protein, E coli; C043296:nickel-iron hydrogenase; D006864:Hydrogenase; D019204:GTP-Binding Proteins; D019696:Peptidylprolyl Isomerase