Dissection of the maturation reactions of the [NiFe] hydrogenase 3 from Escherichia coli taking place after nickel incorporation.
The steps in the maturation of the precursor of the large subunit (pre-HycE) of hydrogenase 3 from Escherichia coli taking place after incorporation of both iron and nickel were investigated. Pre-HycE could be matured and processed in the absence of the small subunit but association with the cytoplasmic membrane required heterodimer formation between the two subunits. Pre-HycE formed a complex with the chaperone-like protein HypC in the absence of the small subunit and, in this complex, also incorporated nickel. For the C-terminal processing, HypC had to leave the complex since only a HypC-free, nickel-containing form of pre-HycE was a substrate for the maturation endopeptidase.
Magalon
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Lehrstuhl für Mikrobiologie der Universität München, Maria-Ward-Strasse 1a, 80638, Munich, Germany.
Böck
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D002458:Cell Fractionation; D010450:Endopeptidases / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology* / Q000378:metabolism; D029968:Escherichia coli Proteins; D005560:Formate Dehydrogenases / Q000378:metabolism; D006864:Hydrogenase / Q000378:metabolism*; D009097:Multienzyme Complexes / Q000378:metabolism; D009532:Nickel / Q000378:metabolism*; D011498:Protein Precursors / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D013347:Subcellular Fractions / Q000201:enzymology
D029968:Escherichia coli Proteins; D009097:Multienzyme Complexes; D011498:Protein Precursors; D009532:Nickel; C086230:hycE protein, E coli; C043296:nickel-iron hydrogenase; D006864:Hydrogenase; D005560:Formate Dehydrogenases; C054017:formate hydrogenlyase; D010450:Endopeptidases