Literature DB >> 19680248

Bacterial cell division: assembly, maintenance and disassembly of the Z ring.

David W Adams1, Jeff Errington.   

Abstract

Bacterial cell division is orchestrated by a tubulin homologue, FtsZ, which polymerizes to form a ring-like structure that is both a scaffold for the assembly of the bacterial cytokinetic machinery and, at least in part, a source of the energy for constriction. FtsZ assembly is tightly regulated, and a diverse repertoire of accessory proteins contributes to the formation of a functional division machine that is responsive to cell cycle status and environmental stress. In this Review, we describe the interaction of these proteins with FtsZ and discuss recent advances in our understanding of Z ring assembly.

Mesh:

Substances:

Year:  2009        PMID: 19680248     DOI: 10.1038/nrmicro2198

Source DB:  PubMed          Journal:  Nat Rev Microbiol        ISSN: 1740-1526            Impact factor:   60.633


  155 in total

1.  Identification and characterization of a negative regulator of FtsZ ring formation in Bacillus subtilis.

Authors:  P A Levin; I G Kurtser; A D Grossman
Journal:  Proc Natl Acad Sci U S A       Date:  1999-08-17       Impact factor: 11.205

2.  MinDE-dependent pole-to-pole oscillation of division inhibitor MinC in Escherichia coli.

Authors:  D M Raskin; P A de Boer
Journal:  J Bacteriol       Date:  1999-10       Impact factor: 3.490

3.  Role of the carboxy terminus of Escherichia coli FtsA in self-interaction and cell division.

Authors:  L Yim; G Vandenbussche; J Mingorance; S Rueda; M Casanova; J M Ruysschaert; M Vicente
Journal:  J Bacteriol       Date:  2000-11       Impact factor: 3.490

4.  Assembly of an FtsZ mutant deficient in GTPase activity has implications for FtsZ assembly and the role of the Z ring in cell division.

Authors:  A Mukherjee; C Saez; J Lutkenhaus
Journal:  J Bacteriol       Date:  2001-12       Impact factor: 3.490

Review 5.  Tubulin and FtsZ form a distinct family of GTPases.

Authors:  E Nogales; K H Downing; L A Amos; J Löwe
Journal:  Nat Struct Biol       Date:  1998-06

6.  SlmA, a nucleoid-associated, FtsZ binding protein required for blocking septal ring assembly over Chromosomes in E. coli.

Authors:  Thomas G Bernhardt; Piet A J de Boer
Journal:  Mol Cell       Date:  2005-05-27       Impact factor: 17.970

7.  A unique cell division machinery in the Archaea.

Authors:  Ann-Christin Lindås; Erik A Karlsson; Maria T Lindgren; Thijs J G Ettema; Rolf Bernander
Journal:  Proc Natl Acad Sci U S A       Date:  2008-11-05       Impact factor: 11.205

8.  Bacillus subtilis EzrA and FtsL synergistically regulate FtsZ ring dynamics during cell division.

Authors:  Yoshikazu Kawai; Naotake Ogasawara
Journal:  Microbiology       Date:  2006-04       Impact factor: 2.777

9.  An altered FtsA can compensate for the loss of essential cell division protein FtsN in Escherichia coli.

Authors:  Christophe S Bernard; Mahalakshmi Sadasivam; Daisuke Shiomi; William Margolin
Journal:  Mol Microbiol       Date:  2007-06       Impact factor: 3.501

10.  SepF, a novel FtsZ-interacting protein required for a late step in cell division.

Authors:  Leendert W Hamoen; Jean-Christophe Meile; Wouter de Jong; Philippe Noirot; Jeff Errington
Journal:  Mol Microbiol       Date:  2006-02       Impact factor: 3.501

View more
  331 in total

1.  A distance-weighted interaction map reveals a previously uncharacterized layer of the Bacillus subtilis spore coat.

Authors:  Peter T McKenney; Adam Driks; Haig A Eskandarian; Paul Grabowski; Jonathan Guberman; Katherine H Wang; Zemer Gitai; Patrick Eichenberger
Journal:  Curr Biol       Date:  2010-05-06       Impact factor: 10.834

2.  Inside-out Z rings--constriction with and without GTP hydrolysis.

Authors:  Masaki Osawa; Harold P Erickson
Journal:  Mol Microbiol       Date:  2011-06-16       Impact factor: 3.501

3.  Sequential closure of the cytoplasm and then the periplasm during cell division in Escherichia coli.

Authors:  Karl Skoog; Bill Söderström; Jerker Widengren; Gunnar von Heijne; Daniel O Daley
Journal:  J Bacteriol       Date:  2011-11-18       Impact factor: 3.490

Review 4.  Nucleoid occlusion and bacterial cell division.

Authors:  Ling Juan Wu; Jeff Errington
Journal:  Nat Rev Microbiol       Date:  2011-10-24       Impact factor: 60.633

5.  FtsA forms actin-like protofilaments.

Authors:  Piotr Szwedziak; Qing Wang; Stefan M V Freund; Jan Löwe
Journal:  EMBO J       Date:  2012-03-30       Impact factor: 11.598

6.  Nucleotide-dependent conformations of FtsZ dimers and force generation observed through molecular dynamics simulations.

Authors:  Jen Hsin; Ajay Gopinathan; Kerwyn C Huang
Journal:  Proc Natl Acad Sci U S A       Date:  2012-05-30       Impact factor: 11.205

7.  RefZ facilitates the switch from medial to polar division during spore formation in Bacillus subtilis.

Authors:  Jennifer K Wagner-Herman; Remi Bernard; Roisin Dunne; Alexandre W Bisson-Filho; Krithika Kumar; Trang Nguyen; Lawrence Mulcahy; John Koullias; Frederico J Gueiros-Filho; David Z Rudner
Journal:  J Bacteriol       Date:  2012-06-22       Impact factor: 3.490

8.  E93R substitution of Escherichia coli FtsZ induces bundling of protofilaments, reduces GTPase activity, and impairs bacterial cytokinesis.

Authors:  Richa Jaiswal; Ronak Y Patel; Jayant Asthana; Bhavya Jindal; Petety V Balaji; Dulal Panda
Journal:  J Biol Chem       Date:  2010-07-28       Impact factor: 5.157

9.  DivIC stabilizes FtsL against RasP cleavage.

Authors:  Inga Wadenpohl; Marc Bramkamp
Journal:  J Bacteriol       Date:  2010-07-19       Impact factor: 3.490

10.  SpyAD, a moonlighting protein of group A Streptococcus contributing to bacterial division and host cell adhesion.

Authors:  Marilena Gallotta; Giovanni Gancitano; Giampiero Pietrocola; Marirosa Mora; Alfredo Pezzicoli; Giovanna Tuscano; Emiliano Chiarot; Vincenzo Nardi-Dei; Anna Rita Taddei; Simonetta Rindi; Pietro Speziale; Marco Soriani; Guido Grandi; Immaculada Margarit; Giuliano Bensi
Journal:  Infect Immun       Date:  2014-04-28       Impact factor: 3.441

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.