Streptococcus pneumoniae DivIVA: Localization and Interactions in a MinCD-Free Context

Author:

Fadda Daniela1,Santona Antonella1,D'Ulisse Valeria2,Ghelardini Patrizia3,Ennas Maria Grazia4,Whalen Michael B.5,Massidda Orietta1

Affiliation:

1. Dipartimento di Scienze e Tecnologie Biomediche, Sez. Microbiologia Medica, Università di Cagliari, Via Porcell, 4, 09100 Cagliari, Italy

2. Dipartimento di Biologia, Università “Tor Vergata,” Via della Ricerca Scientifica, I-00133 Roma, Italy

3. Istituto di Biologia e Patologia Molecolare CNR, Roma, Italy

4. Dipartimento di Citomorfologia, Università di Cagliari, Monserrato, Cagliari, Italy

5. Dipartimento di Bioinformatica, SharDna Life Sciences, 09100 Pula, Cagliari, Italy

Abstract

ABSTRACT To clarify the function of DivIVA in Streptococcus pneumoniae , we localized this protein in exponentially growing cells by both immunofluorescence microscopy and immunoelectron microscopy and found that S. pneumoniae DivIVA (DivIVA SPN ) had a unique localization profile: it was present simultaneously both as a ring at the division septum and as dots at the cell poles. Double-immunofluorescence analysis suggested that DivIVA is recruited to the septum at a later stage than FtsZ and is retained at the poles after cell separation. All the other cell division proteins that we tested were localized in the divIVA null mutant, although the percentage of cells having 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 the possibility of a direct role in chromosome segregation cannot be ruled out, DivIVA in S. pneumoniae seems to be primarily involved in the formation and maturation of the cell poles. The localization and the interaction properties of DivIVA SPN raise the intriguing possibility that a common, MinCD-independent function evolved differently in the various host backgrounds.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

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