Study on post-translational isoprenylation of a tryptophan residue in quorum sensing pheromone

2016 Fiscal Year Final Research Report

• Project/Area Number: 24688011
• Research Category: Grant-in-Aid for Young Scientists (A)
• Allocation Type: Partial Multi-year Fund
• Research Field: Bioproduction chemistry/Bioorganic chemistry
• Research Institution: The University of Tokyo (2014-2016); Chubu University (2012-2013)
• Principal Investigator: Okada Masahiro 東京大学, 薬学研究科(研究院), 准教授 (40377792)
• Project Period (FY): 2012-04-01 – 2017-03-31
• Keywords: クオラムセンシング / 翻訳後修飾 / 枯草菌 / トリプトファン

Outline of Final Research Achievements

Post-translational isoprenylation of a tryptophan residue was first found in a prokaryotes Bacillus subtilis. In order to evaluate the diversity of post-translational isoprenylation, we focused on the modification enzymes. Based on the information of the essential amino acid residues for the isoprenylation activity, a novel Trp-farnesyltransferase and a novel Trp-farnesylated peptide were found in another phyla of bacteria. Then, X-ray crystal analysis of the Trp-farnesyltransferase was carried out, and then genome mining for proteins sharing the structural features of the enzyme revealed that post-translational isoprenylation of tryptophan was widely distributed in several phyla of bacteria.
In addition, a novel Trp-farnesylated peptide involved in the formation of sticky biofilm was found from B. subtilis subsp. natto. Then, detailed farnesylation analyses of the enzyme revealed that post-translationally isoprenylating enzyme for Trp residue exhibited broad substrate tolerance.

Free Research Field

天然物化学