title: Control of cell wall assembly by a histone-like protein in Mycobacteria.
abstract: 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.
authors.affiliation: Department of Host Defense, Osaka City University Graduate School of Medicine, 1-4-3 Asahi-machi, Abeno-ku, Osaka 545-8585, Japan.
authors.forename: Tomoya
authors.initials: T
authors.lastname: Katsube
authors.forename: Sohkichi
authors.initials: S
authors.lastname: Matsumoto
authors.forename: Masaki
authors.initials: M
authors.lastname: Takatsuka
authors.forename: Megumi
authors.initials: M
authors.lastname: Okuyama
authors.forename: Yuriko
authors.initials: Y
authors.lastname: Ozeki
authors.forename: Mariko
authors.initials: M
authors.lastname: Naito
authors.forename: Yukiko
authors.initials: Y
authors.lastname: Nishiuchi
authors.forename: Nagatoshi
authors.initials: N
authors.lastname: Fujiwara
authors.forename: Mamiko
authors.initials: M
authors.lastname: Yoshimura
authors.forename: Takafumi
authors.initials: T
authors.lastname: Tsuboi
authors.forename: Motomi
authors.initials: M
authors.lastname: Torii
authors.forename: Nobuhide
authors.initials: N
authors.lastname: Oshitani
authors.forename: Tetsuo
authors.initials: T
authors.lastname: Arakawa
authors.forename: Kazuo
authors.initials: K
authors.lastname: Kobayashi
mesh_terms: D000217:Acyltransferases / Q000378:metabolism; D018829:Adhesins, Bacterial / Q000378:metabolism; D000942:Antigens, Bacterial / Q000378:metabolism; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D002473:Cell Wall / Q000378:metabolism*; D003311:Cord Factors; D004268:DNA-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial; D006017:Glycolipids; D006657:Histones / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D009163:Mycobacterium bovis; D020102:Mycobacterium smegmatis / Q000166:cytology* / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding
chemical_list: D018829:Adhesins, Bacterial; D000942:Antigens, Bacterial; D001426:Bacterial Proteins; D003311:Cord Factors; D004268:DNA-Binding Proteins; D006017:Glycolipids; D006657:Histones; C403010:MDP1 protein, Mycobacterium; C021099:trehalose monomycolate; D000217:Acyltransferases