Spo0B of Bacillus anthracis - a protein with pleiotropic functions

The FEBS Journal
Abid R MattooYogendra Singh

Abstract

Spo0B is an important component of the phosphorelay signal transduction pathway, the pathway involved in the initiation of sporulation in Bacillus subtilis. Bioinformatic, phylogenetic and biochemical studies showed that Spo0B of Bacillus anthracis has evolved from citrate/malate kinases. During the course of evolution, Spo0B has retained the characteristic histidine kinase boxes H, N, F, G(1) and G(2), and has acquired nucleotide-binding domains, Walker A and Walker B, of ATPases. Owing to the presence of these domains, autophosphorylation and ATPase activity was observed in Spo0B of B. anthracis. Mutational studies showed that among the six histidine residues, His13 of the H-box is involved in the autophosphorylation activity of Spo0B, whereas Lys33 of the Walker A domain is associated with the ATPase activity of the protein. Thermodynamic and binding studies of the binding of Mg-ATP to Spo0B using isothermal titration calorimetry (ITC) suggested that the binding is driven by favorable entropy changes and that the reaction is exothermic, with an apparent dissociation constant (K(d)) equal to 0.02 mm. The value of the dissociation constant (K(d) = 0.05 mm) determined by the intrinsic fluorescence of trytophan of Spo0B was simi...Continue Reading

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Citations

Oct 26, 2011·Microbial Cell Factories·Tjakko AbeeHeidy den Besten
Mar 10, 2010·Journal of Molecular Recognition : JMR·Robert J FalconerBrett M Collins
Aug 19, 2014·Environmental Microbiology Reports·Elena Dalla VecchiaRizlan Bernier-Latmani
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May 5, 2017·Pathogens and Disease·Shikha JoonRakesh Bhatnagar
Apr 16, 2020·Microorganisms·Meng ChenHengliang Wang

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