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The secretion of lecithinase of Pseudomonas alcaligenes S2 was via type II secretion pathway

Science Bulletin 2005年第16期 61-66页

作者： lü jing1, li fan1, chen sanfeng1,2.& li jilun1,3 1. state key laboratory of Agrobiotechnology, china agricultural uni-versity, beijing 100094, china 2. key laboratory of Agro-Microbial Resource and Application in Agri-culture Ministry, china agricultural university, beijing 100094, china 3. College of Biological Sciences, china agricultural university, beijing 100094, china

Strain S2 is a lecithin (or phosphatidylcholine)- solubilizing bacterium, which was isolated from the rice rhizosphere in rural areas of beijing, china. On the basis of a polyphasic study involving phenotypic tests, physiological and biochemical tests, 1.S rDNA sequence analysis, G+C content determination and DNA-DNA hybridizations analy-sis, strain S2 was identified as Pseudomonas alcaligenes. P. alcaligenes S2 was mutagenized with Tn5 and four mutants showing decreased or increased solubilizing ability of lecithin were isolated based on the halo size around colonies on the solid plate supplemented with egg yolk. To characterize the genes of P. alcaligenes S2 involved in solubilization of lecithin, the EcoR I fragments of the chromosomes from the four mutant strains carrying a single transposon were cloned, and the DNA sequences flanking the Tn5 were determined. The Tn5 insertion sites in the mutants M808, M1.29 and M1.00, showing decreased solubilizing ability of lecithin, were found to be located in the xcpS, xcpX and xcpW , respectively, whose products XcpS, XcpX and XcpW were the components of type II secretion pathway. Complementation of xcpS, xcpX and xcpW could restore the corresponding mutants M808, M1.29 and M1.00 to solubilize lecithin. The data suggested that mutation in one of these xcp genes would lead to the absence of mature lecithinase secretion into the extracellular medium. The data also indicated that the secretion of leci-thin-hydrolyzing enzyme of P. alcaligenes was via type II secretion pathway. In the mutant M20 showing increasing lecithin-hydrolyzing activity, the interrupted gene showed 86% identity with chpA of Pseudomonas aeruginosa PAO1. whose product plays an important role in controlling twitch-ing motility of the bacterial cells.

关键词： Pseudomonas alcaligenes mutants lecithin solubilization Tn5.

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The secretion of lecithinase of Pseudomonas alcaligenes S2 was via type II secretion pathway

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Chinese Science Bulletin 2005年第16期50卷 1731-1736页

作者： lU jing {1. fan chen sanfeng {1. jilun state {1. laboratory of Agrobiotecbnology China Agricultural University Beijing 100094 China key {1. of Agro-Microbial Resource and Application in Agriculture Ministry China Agricultural University Beijing 100094China College of Biological Sciences China Agricultural University Beijing 100094 China

关键词：卵磷脂酵素假单胞菌分泌物突变异种生物化学

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