Structure–function analysis of the extracellular domain of the pneumococcal cell division site positioning protein MapZ

Sylvie Manuse, Nicolas L. Jean, Mégane Guinot, Jean-Pierre Lavergne, Cédric Laguri, Catherine M. Bougault, Michael S. VanNieuwenhze, Christophe Grangeasse () and Jean-Pierre Simorre ()
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Sylvie Manuse: CNRS, Molecular Microbiology and Structural Biochemistry
Nicolas L. Jean: Université Grenoble Alpes, Institut de Biologie Structurale
Mégane Guinot: CNRS, Molecular Microbiology and Structural Biochemistry
Jean-Pierre Lavergne: CNRS, Molecular Microbiology and Structural Biochemistry
Cédric Laguri: Université Grenoble Alpes, Institut de Biologie Structurale
Catherine M. Bougault: Université Grenoble Alpes, Institut de Biologie Structurale
Michael S. VanNieuwenhze: Indiana University
Christophe Grangeasse: CNRS, Molecular Microbiology and Structural Biochemistry
Jean-Pierre Simorre: Université Grenoble Alpes, Institut de Biologie Structurale

Nature Communications, 2016, vol. 7, issue 1, 1-13

Abstract: Abstract Accurate placement of the bacterial division site is a prerequisite for the generation of two viable and identical daughter cells. In Streptococcus pneumoniae, the positive regulatory mechanism involving the membrane protein MapZ positions precisely the conserved cell division protein FtsZ at the cell centre. Here we characterize the structure of the extracellular domain of MapZ and show that it displays a bi-modular structure composed of two subdomains separated by a flexible serine-rich linker. We further demonstrate in vivo that the N-terminal subdomain serves as a pedestal for the C-terminal subdomain, which determines the ability of MapZ to mark the division site. The C-terminal subdomain displays a patch of conserved amino acids and we show that this patch defines a structural motif crucial for MapZ function. Altogether, this structure–function analysis of MapZ provides the first molecular characterization of a positive regulatory process of bacterial cell division.

Date: 2016
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DOI: 10.1038/ncomms12071

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