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Journal of Bacteriology, May 2005, p. 3511-3520, Vol. 187, No. 10
0021-9193/05/$08.00+0 doi:10.1128/JB.187.10.3511-3520.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
Sigal Ben-Yehuda,
Nicole King,¶ and
Richard Losick*
Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138
Received 1 December 2004/ Accepted 10 February 2005
SpoIIE is a dual-function protein in Bacillus subtilis that contributes to the switch from medial to polar cell division during sporulation and is responsible for activating the cell-specific transcription factor
F. SpoIIE consists of an N-terminal domain with 10 membrane-spanning segments (region I), a C-terminal phosphatase domain (region III), and a central domain (region II) of uncertain function. To investigate the role of SpoIIE in polar division, we took advantage of a system for efficiently producing polar septa during growth in a SpoIIE-dependent manner using cells engineered to produce the sporulation protein in response to an inducer. The results show that regions II and III play a critical role in polar septum formation and that specific amino acid substitutions in those regions affect the abilities of SpoIIE both to promote polar division and to localize to the division machinery. Additionally, we show that neither the phosphatase function of SpoIIE nor the N-terminal, membrane-spanning region is needed for the switch to asymmetric division.
Supplemental material for this article may be found at http://jb.asm.org/.
Present address: The Schepens Eye Research Institute, Harvard University, 20 Staniford Street, Boston, MA 02114.
Present address: Department of Molecular Biology, Faculty of Medicine, The Hebrew University of Jerusalem, 911120 Jerusalem, Israel.
¶ Present address: Department of Molecular and Cell Biology, University of California, Berkeley, 142 Life Sciences Addition, #3200, Berkeley, CA 94720.
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