Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
Organic Chemistry Communication
Chemical Structure of Posttranslational Modification with A Farnesyl Group on Tryptophan
Masahiro OKADAHisao YAMAGUCHIIsao SATOFumitada TSUJIDavid DUBNAUYouji SAKAGAMI
著者情報
ジャーナル フリー

2008 年 72 巻 3 号 p. 914-918

詳細
抄録
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.
著者関連情報

この記事は最新の被引用情報を取得できません。

© 2008 by Japan Society for Bioscience, Biotechnology, and Agrochemistry
前の記事 次の記事
feedback
Top