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

Autor: Sylvie Manuse, Cédric Laguri, Jean-Pierre Simorre, Michael S. VanNieuwenhze, Jean-Pierre Lavergne, Catherine M. Bougault, Nicolas L. Jean, Mégane Guinot, Christophe Grangeasse
Přispěvatelé: Microbiologie moléculaire et biochimie structurale / Molecular Microbiology and Structural Biochemistry (MMSB), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Institut de biologie structurale (IBS - UMR 5075 ), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Department of Chemistry, Indiana University, Indiana University [Bloomington], Indiana University System-Indiana University System, PLATIM and Protein Sciences platforms of SFR Biosciences Gerland-Lyon Sud (UMS344/US8), NMR and isotope labelling platforms of the Grenoble Instruct Center (ISBG, UMS 3518 CNRS-CEA-UJF-EMBL), ANR-12-BSV3-0008,PiBaKi,Rôle cellulaire et mode d'action de deux protéine-kinases centrales chez les bactéries(2012), ANR-15-CE32-0001,Map-CellDiv,MapZ: caractérisation d'un nouveau mécanisme de régulation de la division cellulaire bactérienne(2015), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)
Jazyk: angličtina
Rok vydání: 2016
Předmět:
MESH: Cytokinesis
0301 basic medicine
Models
Molecular
MESH: Cytoskeletal Proteins
Cell division
Protein Conformation
Science
Protein domain
General Physics and Astronomy
General Biochemistry
Genetics and Molecular Biology
Article
03 medical and health sciences
Structure-Activity Relationship
MESH: Protein Conformation
MESH: Structure-Activity Relationship
Protein structure
Bacterial Proteins
Protein Domains
FtsZ
Cytoskeleton
MESH: Bacterial Proteins
Cytokinesis
MESH: Gene Expression Regulation
Bacterial
Multidisciplinary
[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Structural Biology [q-bio.BM]
biology
General Chemistry
Gene Expression Regulation
Bacterial
Cell cycle
Cell biology
Cytoskeletal Proteins
030104 developmental biology
Streptococcus pneumoniae
Biochemistry
biology.protein
MESH: Cell Division
MESH: Protein Domains
MESH: Models
Molecular
MESH: Streptococcus pneumoniae
Cell Division
Cell division site
Zdroj: Nature Communications, Vol 7, Iss 1, Pp 1-13 (2016)
Nature Communications
Nature Communications, Nature Publishing Group, 2016, 7 (1), pp.12071. ⟨10.1038/ncomms12071⟩
Nature Communications, 2016, 7 (1), pp.12071. ⟨10.1038/ncomms12071⟩
'Nature Communications ', vol: 7, pages: 12071-1-12071-13 (2016)
ISSN: 2041-1723
DOI: 10.1038/ncomms12071⟩
Popis: 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.
Placement of the bacterial division site is crucial for the creation of identical daughter cells. Here, the authors solve the structure of the MapZ protein, which helps to position the cell division protein FtsZ at the cell centre, and further analyse the function of the protein in vivo.
Databáze: OpenAIRE
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