Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451

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Chemical Structure of Posttranslational Modification with A Farnesyl Group on Tryptophan
Masahiro OKADAHisao YAMAGUCHIIsao SATOFumitada TSUJIDavid DUBNAUYouji SAKAGAMI
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ジャーナル フリー 早期公開

論文ID: 80006

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Bacillus subtilis and related bacilli produce a posttranslationally modified oligopeptide, the ComX pheromone, that stimulates natural genetic competence controlled by quorum sensing. The ComXRO-C-2 pheromone from strain RO-C-2 must be modified with a farnesyl group on the Trp residue, but the precise structure is not known. Here we report the precise nature of posttranslational farnesylation of ComXRO-C-2 pheromone on the Trp residue, resulting in the formation of a tricyclic structure. The ComX168 pheromone, produced by the standard laboratory strain used in the study of B. subtilis, is also posttranslationally farnesylated according to phylogenetic resemblance.
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© 2008 by Japan Society for Bioscience, Biotechnology, and Agrochemistry
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