Chemical structure of posttranslational modification with a farnesyl group on tryptophan.
Bacillus subtilis and related bacilli produce a posttranslationally modified oligopeptide, the ComX pheromone, that stimulates natural genetic competence controlled by quorum sensing. The ComX(RO-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 ComX(RO-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.
Okada
Masahiro
M
Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan.
Yamaguchi
Hisao
H
Sato
Isao
I
Tsuji
Fumitada
F
Dubnau
David
D
Sakagami
Youji
Y
D001412:Bacillus subtilis / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D015394:Molecular Structure; D011487:Protein Conformation; D017368:Protein Prenylation; D011499:Protein Processing, Post-Translational; D014364:Tryptophan / Q000378:metabolism*
D001426:Bacterial Proteins; C087040:ComX protein, Bacillus subtilis; D014364:Tryptophan