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Protein‐Protein Interactions in Nickel Acquisition of Escherichia coli
Author(s) -
Zeng Zhi Wei,
Zamble Deborah
Publication year - 2017
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.31.1_supplement.912.8
Subject(s) - nickel , escherichia coli , chemistry , transporter , hydrogenase , biochemistry , bacteria , intracellular , cyclic nucleotide binding domain , nucleotide , transport protein , enzyme , atp hydrolysis , biophysics , biology , atpase , gene , genetics , organic chemistry
Nickel is a required cofactor for [NiFe]‐hydrogenase, an enzyme involved in bacterial metabolism and pathogenesis.1 Due to the toxicity of nickel,2 bacteria need to control its uptake and distribution intracellularly.3 In Escherichia coli , control of intracellular nickel is achieved by nickel uptake by membrane transporters and nickel delivery to the correct destinations by metallochaperone proteins; however, it is not clear how these two systems are linked. Previous results suggested that there is an interaction between the nickel metallochaperone HypB and a nucleotide binding domain of Nik transporter NikE. This protein‐protein interaction would support the hypothesis that HypB, a key protein in nickel delivery to the [NiFe]‐hydrogenase precursor protein, receives nickel directly from the Nik transporter. In the present work, the NikE‐HypB interaction is examined under various nucleotide‐loaded and metal‐loaded states of HypB. Support or Funding Information This work was supported in part by funding from NSERC and CIHR.