TAILIEUCHUNG - Báo cáo khoa học: Spo0B of Bacillus anthracis – a protein with pleiotropic functions

Spo0B is an important component of the phosphorelay signal transduction pathway, the pathway involved in the initiation of sporulation inBacil-lus subtilis. Bioinformatic, phylogenetic and biochemical studies showed that Spo0B of Bacillus anthracishas evolved from citrate⁄malate kinases. | ỊFEBS Journal Spo0B of Bacillus anthracis - a protein with pleiotropic functions Abid R. Mattoo Mohd Saif Zaman Gyanendra P. Dubey Amit Arora Azeet Narayan Noor Jailkhani Kusum Rathore Souvik Maiti and Yogendra Singh Allergy and Infectious Diseases Institute of Genomics and Integrative Biology Delhi India Keywords Bacillus anthracis histidine kinase Spo0B sporulation Symbet Correspondence Y. Singh Institute of Genomics and Integrative Biology MallRoad Delhi 110 007 India Fax 91 11 27667471 Tel 91 11 27666156 E-mail ysingh@ Received 29 October 2007 revised 8 December 2007 accepted 12 December 2007 doi 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 G1 and G2 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 Kd equal to mM. The value of the dissociation constant Kd mM determined by the intrinsic fluorescence of trytophan of Spo0B was similar to that obtained by ITC studies. The purified Spo0B of B. anthracis also showed nucleoside diphosphate kinase-like activity .

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