Bacillus subtilis Spore Coat Protein LipC Is a Phospholipase B

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概要

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• In Bacillus subtilis, the germination-related lipase LipC is located in the spore coat, and mutant spores are defective in L-alanine-stimulated germination. To determine the physiological role of LipC, the recombinant LipC expressed in Escherichia coli was purified and characterized. The enzyme hydrolyzes p-nitrophenyl ester substrates with various acyl-chain lengths. Thin-layer chromatography and gas chromatography-mass spectrometry analysis indicated that LipC cleaves the fatty acids at the sn-1 and sn-2 positions of phospholipids as phospholipase B, and that the enzyme shows no selectivity for the polar head groups of lipid molecules. When the amounts of free fatty acids in dormant wild-type and lipC mutant (YCSKd) spores were measured, the amount of free fatty acids in the YCSKd spores was about 35% less than in the wild-type spores. These results suggest the possibility that Bacillus subtilis LipC plays an important role in the degradation of the outer spore membrane during sporulation.

• 社団法人 日本農芸化学会の論文

著者

• Hemmi Hisashi

  Department Of Biomolecular Engineering Graduate School Of Engineering Tohoku University

• Kato Shiro

  Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya Uni

• Yoshimura Tohru

  Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya Uni

• MORIYAMA Ryuichi

  Department of Food and Nutritional Sciences, College of Bioscience and Biotechnology, Chubu Universi

• Masayama Atsushi

  Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya Uni

• Terashima Takuya

  Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya Uni

• MØLGAARD Anne

  Department of Chemistry, University of Copenhagen

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