PMID:22085337

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Citation

Kaluarachchi, H, Zhang, JW and Zamble, DB (2011) Escherichia coli SlyD, more than a Ni(II) reservoir. Biochemistry 50:10761-3

Abstract

SlyD interacts with HypB and contributes to nickel insertion during [NiFe]-hydrogenase biogenesis. Herein, we provide evidence of SlyD acting as a nickel storage determinant in Escherichia coli and show that this Ni(II) can be mobilized to HypB in vitro even under competitive conditions. Furthermore, SlyD enhances the GTPase activity of HypB, and acceleration of release of Ni(II) from HypB is more pronounced when HypB is GDP-bound. The data support a model in which a HypB-SlyD complex establishes communication between GTP hydrolysis and nickel delivery and provide insight into the role of the HypB-SlyD complex during [NiFe]-hydrogenase biosynthesis.

Links

PubMed PMC3253374 Online version:10.1021/bi201590d

Keywords

Apoproteins/chemistry; Apoproteins/metabolism; Binding Sites; Biocatalysis; Carrier Proteins/chemistry; Carrier Proteins/metabolism; Chelating Agents/chemistry; Escherichia coli/enzymology; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; GTP-Binding Proteins/chemistry; GTP-Binding Proteins/genetics; GTP-Binding Proteins/metabolism; Guanosine Diphosphate/metabolism; Guanosine Triphosphate/metabolism; Hydrogenase/chemistry; Hydrogenase/genetics; Hydrogenase/metabolism; Kinetics; Models, Chemical; Mutant Proteins/chemistry; Mutant Proteins/metabolism; Nickel/chemistry; Nickel/metabolism; Peptide Fragments/chemistry; Peptide Fragments/metabolism; Peptidylprolyl Isomerase/chemistry; Peptidylprolyl Isomerase/genetics; Peptidylprolyl Isomerase/metabolism; Protein Interaction Domains and Motifs; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism; Spectrometry, Mass, Electrospray Ionization

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