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Journal of Bacteriology, August 2006, p. 5541-5550, Vol. 188, No. 15
0021-9193/06/$08.00+0     doi:10.1128/JB.00188-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

A New D,L-Endopeptidase Gene Product, YojL (Renamed CwlS), Plays a Role in Cell Separation with LytE and LytF in Bacillus subtilis

Tatsuya Fukushima,1 Anahita Afkham,1 Shin-ichirou Kurosawa,1 Taichi Tanabe,1 Hiroki Yamamoto,1 and Junichi Sekiguchi1,2*

Department of Applied Biology, Faculty of Textile Science and Technology,1 Division of Gene Research, Department of Life Sciences, Research Center for Human and Environmental Sciences, Shinshu University, 3-15-1 Tokida, Ueda-shi, Nagano 386-8567, Japan2

Received 5 February 2006/ Accepted 12 May 2006

A new peptidoglycan hydrolase, Bacillus subtilis YojL (cell wall-lytic enzyme associated with cell separation, renamed CwlS), exhibits high amino acid sequence similarity to LytE (CwlF) and LytF (CwlE), which are associated with cell separation. The N-terminal region of CwlS has four tandem repeat regions (LysM repeats) predicted to be a peptidoglycan-binding module. The C-terminal region exhibits high similarity to the cell wall hydrolase domains of LytE and LytF at their C-terminal ends. The C-terminal region of CwlS produced in Escherichia coli could hydrolyze the linkage of D-{gamma}-glutamyl-meso-diaminopimelic acid in the cell wall of B. subtilis, suggesting that CwlS is a D,L-endopeptidase. ß-Galactosidase fusion experiments and Northern hybridization analysis suggested that the cwlS gene is transcribed during the late vegetative and early stationary phases. A cwlS mutant exhibited a cell shape similar to that of the wild type; however, a lytE lytF cwlS triple mutant exhibited aggregated microfiber formation. Moreover, immunofluorescence microscopy showed that FLAG-tagged CwlS was localized at cell separation sites and cell poles during the late vegetative phase. The localization sites are similar to those of LytF and LytE, indicating that CwlS is involved in cell separation with LytF and LytE. These specific localizations may be dependent on the LysM repeats in their N-terminal domains. The roles of CwlS, LytF, and LytE in cell separation are discussed.

* Corresponding author. Mailing address: Department of Applied Biology, Faculty of Textile Science and Technology, Shinshu University, 3-15-1 Tokida, Ueda-shi, Nagano 386-8567, Japan. Phone: 81-268-21-5344. Fax: 81-268-21-5345. E-mail: jsekigu{at}giptc.shinshu-u.ac.jp.

Journal of Bacteriology, August 2006, p. 5541-5550, Vol. 188, No. 15
0021-9193/06/$08.00+0     doi:10.1128/JB.00188-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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