title: The bacterial cell division regulators MinD and MinC form polymers in the presence of nucleotide.
abstract: The Min system of proteins, consisting of MinC, MinD and MinE, is essential for normal cell division in Escherichia coli. MinC forms a polar gradient to restrict placement of the division septum to midcell. MinC localization occurs through a direct interaction with MinD, a membrane-associating Par-like ATPase. MinE stimulates ATP hydrolysis by MinD, thereby releasing MinD from the membrane. Here, we show that MinD forms polymers with MinC and ATP without the addition of phospholipids. The topological regulator MinE induces disassembly of MinCD polymers. Two MinD mutant proteins, MinD(K11A) and MinD(ΔMTS15), are unable to form polymers with MinC.
authors.affiliation: Department of Cell and Molecular Biology, The University of Rhode Island, Kingston, RI, USA.
authors.forename: Joseph
authors.initials: J
authors.lastname: Conti
authors.affiliation: Department of Cell and Molecular Biology, The University of Rhode Island, Kingston, RI, USA.
authors.forename: Marissa G
authors.initials: MG
authors.lastname: Viola
authors.affiliation: Department of Cell and Molecular Biology, The University of Rhode Island, Kingston, RI, USA; Department of Nutrition and Food Sciences, The University of Rhode Island, Kingston, RI, USA. Electronic address: cambergj@mail.uri.edu.
authors.forename: Jodi L
authors.initials: JL
authors.lastname: Camberg
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D000255:Adenosine Triphosphate / Q000378:metabolism*; D004926:Escherichia coli / Q000737:chemistry / Q000166:cytology / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D050296:Microbial Viability; D046529:Microscopy, Electron, Transmission; D008958:Models, Molecular; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary
chemical_list: D029968:Escherichia coli Proteins; D008565:Membrane Proteins; C462942:MinC protein, E coli; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; C072069:MinD protein, E coli
keywords: ATPase; Cytokinesis; Min system; MinE; Phospholipids