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Journal of Bacteriology, November 2007, p. 8241-8249, Vol. 189, No. 22
0021-9193/07/$08.00+0     doi:10.1128/JB.00550-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Control of Cell Wall Assembly by a Histone-Like Protein in Mycobacteria{triangledown}

Tomoya Katsube,1,2 Sohkichi Matsumoto,1* Masaki Takatsuka,1,2 Megumi Okuyama,1 Yuriko Ozeki,3 Mariko Naito,4 Yukiko Nishiuchi,1 Nagatoshi Fujiwara,1 Mamiko Yoshimura,1 Takafumi Tsuboi,5 Motomi Torii,6 Nobuhide Oshitani,2 Tetsuo Arakawa,2 and Kazuo Kobayashi7

Department of Host Defense,1 Department of Gastroenterology, Osaka City University Graduate School of Medicine, 1-4-3 Asahi-machi, Abeno-ku, Osaka 545-8585, Japan,2 Sonoda Women's University, 7-29-1 Minamitsukaguchi-cho, Amagasaki, Hyogo, Japan,3 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,4 Cell-Free Science and Technology Research Center and Venture Business Laboratory, Ehime University, 3 Bunkyo-cho, Matsuyama, Ehime 790-8577, Japan,5 Department of Molecular Parasitology, Ehime University Graduate School of Medicine, Toon, Ehime 791-0295, Japan,6 Department of Immunology, National Institute of Infectious Diseases, Toyama 1-23-1, Shinjuku-ku, Tokyo 162-8640, Japan7

Received 11 April 2007/ Accepted 1 September 2007

Bacteria coordinate assembly of the cell wall as well as synthesis of cellular components depending on the growth state. The mycobacterial cell wall is dominated by mycolic acids covalently linked 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 (Ag85) complex proteins. However, the regulation mechanism which links cell wall biogenesis and the growth state has not been elucidated. Here we found that a histone-like protein has a dual concentration-dependent regulatory effect on mycolyltransferase functions of the Ag85 complex through direct binding to both the Ag85 complex and the substrate, trehalose-6-monomycolate, in the cell wall. A histone-like protein-deficient Mycobacterium smegmatis strain has an unusual crenellated cell wall structure and exhibits impaired cessation of glycolipid biosynthesis in the growth-retarded phase. Furthermore, we found that artificial alteration of the amount of the extracellular histone-like protein and the Ag85 complex changes the growth rate of mycobacteria, perhaps due to impaired down-regulation of glycolipid biosynthesis. Our results demonstrate novel regulation of cell wall assembly which has an impact on bacterial growth.

* Corresponding author. Mailing address: Department of Host Defense, Osaka City University Graduate School of Medicine, 1-4-3 Asahi-machi, Abeno-ku, Osaka 545-8585, Japan. Phone: 81-6-6645-3746. Fax: 81-6-6645-3747. E-mail: sohkichi{at}med.osaka-cu.ac.jp

{triangledown} Published ahead of print on 14 September 2007.

Journal of Bacteriology, November 2007, p. 8241-8249, Vol. 189, No. 22
0021-9193/07/$08.00+0     doi:10.1128/JB.00550-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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