title: Identification of a stable complex between a [NiFe]-hydrogenase catalytic subunit and its maturation protease.
abstract: Salmonella enterica serovar Typhimurium has the ability to use molecular hydrogen as a respiratory electron donor. This is facilitated by three [NiFe]-hydrogenases termed Hyd-1, Hyd-2, and Hyd-5. Hyd-1 and Hyd-5 are homologous oxygen-tolerant [NiFe]-hydrogenases. A critical step in the biosynthesis of a [NiFe]-hydrogenase is the proteolytic processing of the catalytic subunit. In this work, the role of the maturation protease encoded within the Hyd-5 operon, HydD, was found to be partially complemented by the maturation protease encoded in the Hyd-1 operon, HyaD. In addition, both maturation proteases were shown to form stable complexes, in vivo and in vitro, with the catalytic subunit of Hyd-5. The protein-protein interactions were not detectable in a strain that could not make the enzyme metallocofactor.
authors.affiliation: School of Life Sciences, University of Dundee, UK.
authors.forename: Marta
authors.initials: M
authors.lastname: Albareda
authors.affiliation: School of Life Sciences, University of Dundee, UK.
authors.forename: Grant
authors.initials: G
authors.lastname: Buchanan
authors.affiliation: School of Life Sciences, University of Dundee, UK.
authors.forename: Frank
authors.initials: F
authors.lastname: Sargent
mesh_terms: D000693:Anaerobiosis; D020134:Catalytic Domain; D002876:Chromosomes, Bacterial / Q000378:metabolism; D010450:Endopeptidases / Q000378:metabolism*; D000939:Epitopes / Q000378:metabolism; D056426:Genetic Loci; D006864:Hydrogenase / Q000378:metabolism*; D011485:Protein Binding; D015202:Protein Engineering; D021122:Protein Subunits / Q000378:metabolism; D019779:Salmonella enterica / Q000201:enzymology*; D020798:Two-Hybrid System Techniques
chemical_list: D000939:Epitopes; D021122:Protein Subunits; C043296:nickel-iron hydrogenase; D006864:Hydrogenase; D010450:Endopeptidases
keywords: Salmonella enterica; [NiFe]-hydrogenase, protein-protein interactions; anaerobic respiration; bacterial hydrogen metabolism; metalloenzyme biosynthesis