TAILIEUCHUNG - Báo cáo khoa học: Identification, characterization and activation mechanism of a tyrosine kinase of Bacillus anthracis

Bacillus subtilishas three active tyrosine kinases, PtkA, PtkB and McsB, which play an important role in the physiology of the bacterium. Genome sequence analysis and biochemical experiments indicated that the ortholog of McsB, BAS0080, is the only active tyrosine kinase present inBacillus anthracis. | ỊFEBS Journal Identification characterization and activation mechanism of a tyrosine kinase of Bacillus anthracis Abid R. Mattoo Amit Arora Souvik Maiti and Yogendra Singh Institute of Genomics and Integrative Biology Delhi India Keywords Bacillus anthracis ITC McsB SPR tyrosine kinase Correspondence S. Maiti and Y. Singh Institute of Genomics and Integrative Biology MallRoad Delhi 110 007 India Fax 91 11 27667471 Tel 91 11 27666156 E-mail souvik@ ysingh@ Received 19 August 2008 revised 13 October 2008 accepted 17 October 2008 doi Bacillus subtilis has three active tyrosine kinases PtkA PtkB and McsB which play an important role in the physiology of the bacterium. Genome sequence analysis and biochemical experiments indicated that the ortholog of McsB BAS0080 is the only active tyrosine kinase present in Bacillus anthracis. The autophosphorylation of McsB of B. anthracis was enhanced in the presence of an activator protein McsA BAS0079 a property similar to that reported for B. subtilis. However the process of enhanced phosphorylation of McsB in the presence of McsA remains elusive. To understand the activation mechanism of McsB we carried out spectroscopic and calorimetric experiments with McsB and McsA. The spectroscopic results suggest that the binding affinity of Mg-ATP for McsB increased by one order from 103 to 104 in the presence of McsA. The calorimetric experiments revealed that the interaction between McsB and McsA is endothermic in nature with unfavourable positive enthalpy AH and favourable entropy AS changes leading to an overall favourable free energy change AG . Kinetics of binding of both ATP and McsA with McsB showed low association rates ka and fast dissociation rates kd . These results suggest that enhanced phosphorylation of McsB in the presence of McsA is due to increased affinity of ATP for McsB. Serine threonine and tyrosine protein kinases represent an emerging concept in prokaryotic .

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