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Biosci Biotechnol Biochem

Title:		Post-translational isoprenylation of tryptophan
Author(s):		Okada M;
Address:		"Department of Chemistry, Graduate School of Science, Tohoku University, Aooba-ku, Sendai, Japan. okada@isc.chubu.ac.jp"
Journal Title:		Biosci Biotechnol Biochem
Year:		2011
Volume:		20110807
Issue:		8
Page Number:		1413 - 1417
DOI:		10.1271/bbb.110087
ISSN/ISBN:		1347-6947 (Electronic) 0916-8451 (Linking)
Abstract:		"Bacillus subtilis and related bacilli produce a post-translationally modified oligopeptide, ComX pheromone, that stimulates natural genetic competence controlled by quorum sensing. The ComX pheromones are formed by geranylation or farnesylation on a tryptophan residue at the 3 position of its indole ring. This results in the formation of a tricyclic structure including, a newly formed five-membered ring, similar to proline. Isoprenylation of ComX to form ComX pheromones is essential for pheromonal activity, and is functionally more crucial than its amino acid sequence. The ComX pheromone is the first example of isoprenoidal modifiations of tryptophan residues in living organisms and post-translational isoprenylation of any amino acid in prokaryotes. Because the presence of geranylated compounds is unusual in primary and secondary metabolites outside the plant kingdom, post-translational geranylation in bacilli is unprecedented in nature"
Keywords:		Amino Acid Sequence Bacillus subtilis/genetics/*metabolism Bacterial Proteins/chemistry/genetics/*metabolism Membrane Proteins/chemistry/genetics/*metabolism Molecular Sequence Data Pheromones/chemistry/genetics/*metabolism *Protein Prenylation *Quorum Se;
Notes:		"MedlineOkada, Masahiro eng Review England 2011/08/09 Biosci Biotechnol Biochem. 2011; 75(8):1413-7. doi: 10.1271/bbb.110087. Epub 2011 Aug 7"