Chemical structure of posttranslational modification with a farnesyl group on tryptophan

• Published in: Bioscience, biotechnology, and biochemistry Vol. 72; no. 3; pp. 914 - 918
• Main Authors: Okada, M.(Nagoya Univ. (Japan)), Yamaguchi, H, Sato, I, Tsuji, F, Dubnau, D, Sakagami, Y
• Format: Journal Article
• Language: English
• Published: Tokyo Japan Society for Bioscience, Biotechnology, and Agrochemistry 01.03.2008; Japan Society for Bioscience Biotechnology and Agrochemistry; Oxford University Press
• Subjects: Bacillus; BACILLUS SUBTILIS; Bacillus subtilis - metabolism; Bacterial Proteins - chemistry; Bacterial Proteins - metabolism; Biological and medical sciences; ComX; FEROMONAS; FILOGENIA; Fundamental and applied biological sciences. Psychology; Molecular Structure; PEPTIDE; PEPTIDES; PEPTIDOS; PHEROMONE; PHEROMONES; PHYLOGENIE; PHYLOGENY; posttranslational modification; Protein Conformation; Protein Prenylation; Protein Processing, Post-Translational; PROTEINAS RECOMBINANTES; PROTEINE RECOMBINANTE; quorum sensing; RECOMBINANT PROTEINS; TRIPTOFANO; TRYPTOPHAN; Tryptophan - metabolism; TRYPTOPHANE; Posttranslational modification; Bacillales; Bacillus; Chemical structure; ComX; Tryptophan; Bacteria; Quorum sensing; Bacillaceae
• ISSN: 0916-8451; 1347-6947
• DOI: 10.1271/bbb.80006

Bacillus subtilis and related bacilli produce a posttranslationally modified oligopeptide, the ComX pheromone, that stimulates natural genetic competence controlled by quorum sensing. The ComXsub(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 ComXsub(RO-C-2) pheromone on the Trp residue, resulting in the formation of a tricyclic structure. The ComXsub(168) pheromone, produced by the standard laboratory strain used in the study of B. subtilis, is also posttranslationally farnesylated according to phylogenetic resemblance.