The ArcB Sensor Kinase of Escherichia coli Autophosphorylates by an Intramolecular Reaction | Zendy

Gabriela R. Peña-Sandoval | Zendy; Dimitris Georgellis | Zendy

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The ArcB Sensor Kinase of Escherichia coli Autophosphorylates by an Intramolecular Reaction

Author(s) -

Gabriela R. Peña-Sandoval,

Dimitris Georgellis

Publication year - 2010

Publication title -

journal of bacteriology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.652

H-Index - 246

eISSN - 1067-8832

pISSN - 0021-9193

DOI - 10.1128/jb.01401-09

Subject(s) - autophosphorylation , biology , intramolecular force , response regulator , histidine kinase , kinase , histidine , cytosol , cysteine , intermolecular force , biochemistry , microbiology and biotechnology , protein kinase a , gene , stereochemistry , enzyme , chemistry , bacterial protein , molecule , organic chemistry

The Arc two-component system, comprising the ArcB sensor kinase and the ArcA response regulator, modulates the expression of numerous genes in response to the respiratory conditions of growth. ArcB is a tripartite histidine kinase whose activity is regulated by the oxidation of two cytosol-located redox-active cysteine residues that participate in intermolecular disulfide bond formation. Here we show that ArcB autophosphorylates through an intramolecular reaction which diverges from the usually envisaged intermolecular autophosphorylation of homodimeric histidine kinases.

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