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J. Bacteriol. doi:10.1128/JB.00550-07
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Control of cell wall assembly by a histone-like protein in mycobacteria

Department of Host Defense, and Department of Gastroenterology, Osaka City University Graduate School of Medicine, 1-4-3 Asahi-machi, Abeno-ku, Osaka 545-8585, Japan; Sonoda Womens' University, 7-29-1 Minamitsukaguchi-cho, Amagasaki, Hyogo, Japan; Division of Microbiology and Oral Infection, Department of Molecular Microbiology and Immunology, Nagasaki University Graduate School of Biomedical Sciences, 1-7-1 Sakamoto, Nagasaki 852-8588, Japan; Cell-free Science and Technology Research Center, and Venture Business Laboratory, Ehime University, 3 Bunkyo-cho, Matsuyama, Ehime 790-8577, Japan; Department of Molecular Parasitology, Ehime University Graduate School of Medicine, Toon, Ehime 791-0295, Japan; Department of Immunology, National Institute of Infectious Diseases, Toyama 1-23-1, Shinjuku-ku, Tokyo 162-8640, Japan

^* To whom correspondence should be addressed. Email: sohkichi{at}med.osaka-cu.ac.jp.

	Abstract

Bacteria coordinate assembly of the cell wall as well as synthesis of cellular components depending on growth states. Mycobacterial cell wall is dominated by covalently linked mycolic acids to sugars such as trehalose and arabinose and is critical for pathogenesis of mycobacteria. Transfer of mycolic acids to sugars is necessary for cell wall biogenesis and is mediated by mycolyltransferases, which have been previously identified as three Antigen 85 complex proteins. However, regulation mechanism, which links cell wall biogenesis and growth state, has not been elucidated. Here we found that a histone-like protein has a dual concentration-dependant regulatory activity on mycolyltransferase functions of Ag85 complex through direct binding to both Ag85 complex and their substrate, trehalose 6-monomycolate, in the cell wall. A histone-like protein-deficient Mycobacterium smegmatis displays unusual crenellated cell wall structure and impaired cessation of glycolipids biosyntheses at growth-retarded phase. Furthermore, we showed that artificial alteration of the amount of extracellular histone-like protein and antigen 85 complex changes the growth rate of mycobacteria, perhaps due to impaired down-regulation of glycolipids biosyntheses at growth-retarded phase. Our results demonstrate a novel regulation of cell wall assembly, which has an impact on bacterial growth.

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