| Title: | Chemical structure of posttranslational modification with a farnesyl group on tryptophan |
| Author(s): | Okada M; Yamaguchi H; Sato I; Tsuji F; Dubnau D; Sakagami Y; |
| Address: | "Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan" |
| Journal Title: | Biosci Biotechnol Biochem |
| ISSN/ISBN: | 1347-6947 (Electronic) 0916-8451 (Linking) |
| Abstract: | "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" |
| Keywords: | "Bacillus subtilis/*metabolism Bacterial Proteins/*chemistry/metabolism Molecular Structure Protein Conformation *Protein Prenylation *Protein Processing, Post-Translational Tryptophan/*metabolism;" |
| Notes: | "MedlineOkada, Masahiro Yamaguchi, Hisao Sato, Isao Tsuji, Fumitada Dubnau, David Sakagami, Youji eng R01 GM057720/GM/NIGMS NIH HHS/ GM057720/GM/NIGMS NIH HHS/ Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't England 2008/03/08 Biosci Biotechnol Biochem. 2008 Mar; 72(3):914-8. doi: 10.1271/bbb.80006. Epub 2008 Mar 7" |
