Chemical structure of posttranslational modification with a Farnesyl group on tryptophan
Chemical structure of posttranslational modification with a Farnesyl group on tryptophan
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DOI:
10.1271/bbb.80006
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发表时间:
2008-03-01
影响因子:
1.6
通讯作者:
Sakagami, Youji
中科院分区:
文献类型:
--
作者:
Okada, Masahiro;Yamaguchi, Hisao;Sakagami, Youji
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 ComX(168) pheromone, produced by the, standard laboratory strain used in the study of B. subtilis, is. also posttranslationally farnesylated according to phylogenetic resemblance.