Article abstract
Nature Chemical Biology 4, 766 - 772 (2008)
Published online: 9 November 2008 | doi:10.1038/nchembio.125
-Poly-L-lysine dispersity is controlled by a highly unusual nonribosomal peptide synthetase
Kazuya Yamanaka1,4, Chitose Maruyama2,3, Hiroshi Takagi2,3 & Yoshimitsu Hamano2,4
Abstract
-Poly-L-lysine (-PL) consists of 25–35 L-lysine residues in isopeptide linkages and is one of only two amino acid homopolymers known in nature. Elucidating the biosynthetic mechanism of -PL should open new avenues for creating novel classes of biopolymers. Here we report the purification of an -PL synthetase (Pls; 130 kDa) and the cloning of its gene from an -PL–producing strain of Streptomyces albulus. Pls was found to be a membrane protein with adenylation and thiolation domains characteristic of the nonribosomal peptide synthetases (NRPSs). It had no traditional condensation or thioesterase domain; instead, it had six transmembrane domains surrounding three tandem soluble domains. These tandem domains iteratively catalyzed L-lysine polymerization using free L-lysine polymer (or monomer in the initial reaction) as acceptor and Pls-bound L-lysine as donor, directly yielding chains of diverse length. Thus, Pls is a new single-module NRPS having an amino acid ligase–like catalytic activity for peptide bond formation.
- Yokohama Research Center, Chisso Corporation, 5-1 Ookawa, Kanazawa-Ku, Yokohama 236-8605, Japan.
- Department of Bioscience, Fukui Prefectural University, 4-1-1 Matsuoka-Kenjojima, Eiheiji-cho, Yoshida-gun, Fukui 910-1195, Japan.
- Present addresses: Faculty of Medical Sciences, University of Fukui, 23-3 Matsuoka-shimoaizuki, Eiheiji-cho, Yoshida-gun, Fukui 910-1193, Japan (C.M.) and Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan (H.T.).
- These authors contributed equally to this work.
Correspondence to: Yoshimitsu Hamano2,4 e-mail: hamano@fpu.ac.jp
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