This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental material
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Tavares, J. R.
Right arrow Articles by Gueiros-Filho, F. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Tavares, J. R.
Right arrow Articles by Gueiros-Filho, F. J.

 Previous Article  |  Next Article 

Journal of Bacteriology, November 2008, p. 7096-7107, Vol. 190, No. 21
0021-9193/08/$08.00+0     doi:10.1128/JB.00064-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Cytological Characterization of YpsB, a Novel Component of the Bacillus subtilis Divisome{triangledown} ,{dagger}

José Roberto Tavares, Robson F. de Souza, Guilherme Louzada Silva Meira, and Frederico J. Gueiros-Filho*

Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo, São Paulo, Brazil

Received 13 January 2008/ Accepted 25 August 2008

Cell division in bacteria is carried out by an elaborate molecular machine composed of more than a dozen proteins and known as the divisome. Here we describe the characterization of a new divisome protein in Bacillus subtilis called YpsB. Sequence comparisons and phylogentic analysis demonstrated that YpsB is a paralog of the division site selection protein DivIVA. YpsB is present in several gram-positive bacteria and likely originated from the duplication of a DivIVA-like gene in the last common ancestor of bacteria of the orders Bacillales and Lactobacillales. We used green fluorescent protein microscopy to determine that YpsB localizes to the divisome. Similarly to that for DivIVA, the recruitment of YpsB to the divisome requires late division proteins and occurs significantly after Z-ring formation. In contrast to DivIVA, however, YpsB is not retained at the newly formed cell poles after septation. Deletion analysis suggests that the N terminus of YpsB is required to target the protein to the divisome. The high similarity between the N termini of YpsB and DivIVA suggests that the same region is involved in the targeting of DivIVA. YpsB is not essential for septum formation and does not appear to play a role in septum positioning. However, a ypsB deletion has a synthetic effect when combined with a mutation in the cell division gene ftsA. Thus, we conclude that YpsB is a novel B. subtilis cell division protein whose function has diverged from that of its paralog DivIVA.


* Corresponding author. Mailing address: Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo, Av. Prof. Lineu Prestes 748, 05508-000 São Paulo, SP, Brazil. Phone: 55-11-3091-8520. Fax: 55-11-3091-2186. E-mail: fgueiros{at}iq.usp.br

{triangledown} Published ahead of print on 5 September 2008.

{dagger} Supplemental material for this article may be found at http://jb.asm.org/.


Journal of Bacteriology, November 2008, p. 7096-7107, Vol. 190, No. 21
0021-9193/08/$08.00+0     doi:10.1128/JB.00064-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.