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J. Bacteriol. doi:10.1128/JB.01168-06
Copyright (c) 2006, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Streptococcus pneumoniae DivIVA: localization and interactions in a MinCD free context

Dipartimento di Scienze e Tecnologie Biomediche, Sez. Microbiologia Medica. Università di Cagliari. Via Porcell, 4. 09100 Cagliari. Italy; Dipartimento di Biologia, Università "Tor Vergata", Via della Ricerca Scientifica, I-00133 Roma, Italy; Istituto di Biologia e Patologia Molecolare CNR, Roma, Italy; Dipartimento di Citomorfologia. Università di Cagliari; Monserrato. Cagliari. Italy, Dipartimento di Bioinformatica, SharDna Life Sciences, 09100 Pula, Cagliari. Italy

^* To whom correspondence should be addressed. Email: omassid{at}unica.it.

	Abstract

To clarify the function of DivIVA in S. pneumoniae, we localized the protein in exponentially growing cells, by both immunofluorescence and immunoelectronmicroscopy, and found that DivIVA_SPN showed an unique localization profile, being present simultaneously both as a ring at the division septum and as dots at the cell poles. Double-immunofluorescence suggests that DivIVA is recruited to the septum at a later stage with respect to FtsZ and is retained at the poles after cell separation. All the other cell division proteins that we have tested were localized in the divIVA null mutant, although the percentage of cells showing constricted Z-rings was significantly reduced. In agreement with its localization profile and consistent with its coiled-coil nature, DivIVA interacted with itself and with a number of known or putative S. pneumoniae cell division proteins. Finally, a missense divIVA mutant, obtained by allelic replacement, allowed us to correlate, at the molecular level, the specific interactions and some of the facets of the divIVA mutant phenotype. Taken together the results suggest that, although a direct role in chromosome segregation can not be ruled out, DivIVA in S. pneumoniae seems primarly involved in the formation and maturation of the cell poles. The localization and the interaction properties of DivIVA_SPN raise the intriguing possibility of a common, MinCD independent function, that eventually evolved differently in the various host backgrounds.

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