Abnormal morphology of Bacillus subtilis ugtP mutant cells lacking glucolipids

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  • Matsuoka Satoshi
    Department of Biochemistry and Molecular Biology, Graduate School of Science and Engineering, Saitama University
  • Chiba Minako
    Department of Biochemistry and Molecular Biology, Graduate School of Science and Engineering, Saitama University
  • Tanimura Yu
    Department of Biochemistry and Molecular Biology, Graduate School of Science and Engineering, Saitama University
  • Hashimoto Michihiro
    Department of Biochemistry and Molecular Biology, Graduate School of Science and Engineering, Saitama University
  • Hara Hiroshi
    Department of Biochemistry and Molecular Biology, Graduate School of Science and Engineering, Saitama University
  • Matsumoto Kouji
    Department of Biochemistry and Molecular Biology, Graduate School of Science and Engineering, Saitama University

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Abstract

Bacillus subtilis Marburg 168 cells with disrupted ugtP, which encodes UDP-glucosyltransferase involved in glucolipid synthesis, were bent and distended. In the ugtP mutant cells, the extracytoplasmic function sigmas SigM, SigV and SigX, were found to be activated. Introduction of a disrupted allele of sigM into the ugtP strain caused even more abnormal morphology, with cells taking on a balloon-like shape; growth of these cells in LB medium was hampered by addition of 1.5% NaCl. Addition of MgSO4 or MnCl2 suppressed the abnormal morphology. In ugtP mutant cells the transcription of the mreB operon from an upstream promoter in maf (designated Pupstream mreB) and PmreBH was 4.3- and 2.3-fold higher, respectively, and localization of GFP-MreB was not in discrete dots (in an apparently helical pattern), but faint and in irregular clusters. GFP-MreB protein was reduced in the ugtP mutant cells. We suggest that glucolipids are important for MreB isoforms to take on the configuration that appears as discrete dots and plays a role in shaping cells into straight rods.<br>

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