Literature DB >> 15101985

EzrA prevents aberrant cell division by modulating assembly of the cytoskeletal protein FtsZ.

Daniel P Haeusser1, Rachel L Schwartz, Alison M Smith, Michelle Erin Oates, Petra Anne Levin.   

Abstract

In response to a cell cycle signal, the cytoskeletal protein FtsZ assembles into a ring structure that establishes the location of the division site and serves as a framework for assembly of the division machinery. A battery of factors control FtsZ assembly to ensure that the ring forms in the correct position and at the precise time. EzrA, a negative regulator of FtsZ ring formation, is important for ensuring that the ring forms only once per cell cycle and that cytokinesis is restricted to mid-cell. EzrA is distributed throughout the plasma membrane and localizes to the ring in an FtsZ-dependent manner, suggesting that it interacts directly with FtsZ to modulate assembly. We have performed a series of experiments examining the interaction between EzrA and FtsZ. As little as twofold overexpression of EzrA blocks FtsZ ring formation in a sensitized genetic background, consistent with its predicted function. A purified EzrA fusion protein interacts directly with FtsZ to block assembly in vitro. Although EzrA is able to inhibit FtsZ assembly, it is unable to disassemble preformed polymers. These data support a model in which EzrA interacts directly with FtsZ at the plasma membrane to prevent polymerization and aberrant FtsZ ring formation.

Mesh:

Substances:

Year:  2004        PMID: 15101985      PMCID: PMC5517308          DOI: 10.1111/j.1365-2958.2004.04016.x

Source DB:  PubMed          Journal:  Mol Microbiol        ISSN: 0950-382X            Impact factor:   3.501


  55 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.  Polymerization of Ftsz, a bacterial homolog of tubulin. is assembly cooperative?

Authors:  L Romberg; M Simon; H P Erickson
Journal:  J Biol Chem       Date:  2001-01-04       Impact factor: 5.157

3.  Tubulin-like protofilaments in Ca2+-induced FtsZ sheets.

Authors:  J Löwe; L A Amos
Journal:  EMBO J       Date:  1999-05-04       Impact factor: 11.598

4.  Crystal structure of the SOS cell division inhibitor SulA and in complex with FtsZ.

Authors:  Suzanne C Cordell; Elva J H Robinson; Jan Lowe
Journal:  Proc Natl Acad Sci U S A       Date:  2003-06-13       Impact factor: 11.205

5.  Characterization of the essential cell division gene ftsL(yIID) of Bacillus subtilis and its role in the assembly of the division apparatus.

Authors:  R A Daniel; E J Harry; V L Katis; R G Wake; J Errington
Journal:  Mol Microbiol       Date:  1998-07       Impact factor: 3.501

6.  Direct binding of FtsZ to ZipA, an essential component of the septal ring structure that mediates cell division in E. coli.

Authors:  C A Hale; P A de Boer
Journal:  Cell       Date:  1997-01-24       Impact factor: 41.582

7.  Protein prenylation, et cetera: signal transduction in two dimensions.

Authors:  M H Gelb
Journal:  Science       Date:  1997-03-21       Impact factor: 47.728

8.  In vivo effects of sporulation kinases on mutant Spo0A proteins in Bacillus subtilis.

Authors:  J D Quisel; W F Burkholder; A D Grossman
Journal:  J Bacteriol       Date:  2001-11       Impact factor: 3.490

9.  The FtsZ protein of Bacillus subtilis is localized at the division site and has GTPase activity that is dependent upon FtsZ concentration.

Authors:  X Wang; J Lutkenhaus
Journal:  Mol Microbiol       Date:  1993-08       Impact factor: 3.501

10.  Localization of FtsI (PBP3) to the septal ring requires its membrane anchor, the Z ring, FtsA, FtsQ, and FtsL.

Authors:  D S Weiss; J C Chen; J M Ghigo; D Boyd; J Beckwith
Journal:  J Bacteriol       Date:  1999-01       Impact factor: 3.490

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  54 in total

1.  Fluorescent reporters for studies of cellular localization of proteins in Staphylococcus aureus.

Authors:  Pedro M Pereira; Helena Veiga; Ana M Jorge; Mariana G Pinho
Journal:  Appl Environ Microbiol       Date:  2010-05-07       Impact factor: 4.792

Review 2.  FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one.

Authors:  Harold P Erickson; David E Anderson; Masaki Osawa
Journal:  Microbiol Mol Biol Rev       Date:  2010-12       Impact factor: 11.056

Review 3.  The bacterial divisome: ready for its close-up.

Authors:  Veronica W Rowlett; William Margolin
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  2015-10-05       Impact factor: 6.237

4.  Cell division in Bacillus subtilis: FtsZ and FtsA association is Z-ring independent, and FtsA is required for efficient midcell Z-Ring assembly.

Authors:  S O Jensen; L S Thompson; E J Harry
Journal:  J Bacteriol       Date:  2005-09       Impact factor: 3.490

Review 5.  FtsZ and the division of prokaryotic cells and organelles.

Authors:  William Margolin
Journal:  Nat Rev Mol Cell Biol       Date:  2005-11       Impact factor: 94.444

Review 6.  The bacterial cytoskeleton.

Authors:  Yu-Ling Shih; Lawrence Rothfield
Journal:  Microbiol Mol Biol Rev       Date:  2006-09       Impact factor: 11.056

7.  The division inhibitor EzrA contains a seven-residue patch required for maintaining the dynamic nature of the medial FtsZ ring.

Authors:  Daniel P Haeusser; Anna Cristina Garza; Amy Z Buscher; Petra Anne Levin
Journal:  J Bacteriol       Date:  2007-09-14       Impact factor: 3.490

8.  An FtsZ-targeting prodrug with oral antistaphylococcal efficacy in vivo.

Authors:  Malvika Kaul; Lilly Mark; Yongzheng Zhang; Ajit K Parhi; Edmond J Lavoie; Daniel S Pilch
Journal:  Antimicrob Agents Chemother       Date:  2013-09-16       Impact factor: 5.191

9.  The conserved DNA-binding protein WhiA is involved in cell division in Bacillus subtilis.

Authors:  Katarina Surdova; Pamela Gamba; Dennis Claessen; Tjalling Siersma; Martijs J Jonker; Jeff Errington; Leendert W Hamoen
Journal:  J Bacteriol       Date:  2013-10-04       Impact factor: 3.490

10.  Adenine nucleotide-dependent regulation of assembly of bacterial tubulin-like FtsZ by a hypermorph of bacterial actin-like FtsA.

Authors:  Tushar K Beuria; Srinivas Mullapudi; Eugenia Mileykovskaya; Mahalakshmi Sadasivam; William Dowhan; William Margolin
Journal:  J Biol Chem       Date:  2009-03-17       Impact factor: 5.157

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