Characterization of sporulation histidine kinases of Paenibacillus polymyxa

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Characterization of sporulation histidine kinases of Paenibacillus polymyxa
Soo-Young Park; Seung Hwan Park; Soo Keun Choi
Bibliographic Citation
Research in Microbiology, vol. 163, no. 4, pp. 272-278
Publication Year
Sporulation histidine kinases, which sense sporulation-specific signals and initiate phosphorelay reactions, are poorly conserved among . Bacillus species. We found several putative genes for sporulation histidine kinases in the genome sequence of . Paenibacillus polymyxa E681 and assayed the genes for complementation of sporulation mutants of . Bacillus subtilis. One of these genes, Kin1377, significantly restored the sporulation deficiency of . kinA kinB double mutant of . B. . subtilis, but not of . B. . subtilis spo0B mutant. These results indicated that Kin1377 requires . B. . subtilis Spo0B and possibly Spo0F to transfer phosphate to . B. . subtilis Spo0A. Another putative kinase, Kin1038, slightly restored the sporulation deficiencies of both . kinA kinB double mutant and . spo0B mutant of . B. . subtilis. However the sporulation deficiency of the . B. . subtilis spo0B mutant was significantly restored in the presence of both Kin1038 and . P. . polymyxa Spo0A. These results indicate that the overexpressed Kin1038 is able to interact directly with and activate . P. . polymyxa Spo0A, and that Spo0A can support spore formation in . B. . subtilis.
Histidine kinasePaenibacillus polymyxaPhosphorelaySporulation
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Division of Research on National Challenges > Infectious Disease Research Center > 1. Journal Articles
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