Literature DB >> 9882666

Septal localization of FtsQ, an essential cell division protein in Escherichia coli.

J C Chen1, D S Weiss, J M Ghigo, J Beckwith.   

Abstract

Septation in Escherichia coli requires several gene products. One of these, FtsQ, is a simple bitopic membrane protein with a short cytoplasmic N terminus, a membrane-spanning segment, and a periplasmic domain. We have constructed a merodiploid strain that expresses both FtsQ and the fusion protein green fluorescent protein (GFP)-FtsQ from single-copy chromosomal genes. The gfp-ftsQ gene complements a null mutation in ftsQ. Fluorescence microscopy revealed that GFP-FtsQ localizes to the division site. Replacing the cytoplasmic and transmembrane domains of FtsQ with alternative membrane anchors did not prevent the localization of the GFP fusion protein, while replacing the periplasmic domain did, suggesting that the periplasmic domain is necessary and sufficient for septal targeting. GFP-FtsQ localization to the septum depended on the cell division proteins FtsZ and FtsA, which are cytoplasmic, but not on FtsL and FtsI, which are bitopic membrane proteins with comparatively large periplasmic domains. In addition, the septal localization of ZipA apparently did not require functional FtsQ. Our results indicate that FtsQ is an intermediate recruit to the division site.

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Year:  1999        PMID: 9882666      PMCID: PMC93406     

Source DB:  PubMed          Journal:  J Bacteriol        ISSN: 0021-9193            Impact factor:   3.490


  39 in total

1.  FtsL, an essential cytoplasmic membrane protein involved in cell division in Escherichia coli.

Authors:  L M Guzman; J J Barondess; J Beckwith
Journal:  J Bacteriol       Date:  1992-12       Impact factor: 3.490

2.  Localization of the Escherichia coli cell division protein Ftsl (PBP3) to the division site and cell pole.

Authors:  D S Weiss; K Pogliano; M Carson; L M Guzman; C Fraipont; M Nguyen-Distèche; R Losick; J Beckwith
Journal:  Mol Microbiol       Date:  1997-08       Impact factor: 3.501

3.  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

4.  The membrane-bound cell division protein DivIB is localized to the division site in Bacillus subtilis.

Authors:  E J Harry; R G Wake
Journal:  Mol Microbiol       Date:  1997-07       Impact factor: 3.501

Review 5.  Bacterial cell division and the Z ring.

Authors:  J Lutkenhaus; S G Addinall
Journal:  Annu Rev Biochem       Date:  1997       Impact factor: 23.643

6.  Interactions between heterologous FtsA and FtsZ proteins at the FtsZ ring.

Authors:  X Ma; Q Sun; R Wang; G Singh; E L Jonietz; W Margolin
Journal:  J Bacteriol       Date:  1997-11       Impact factor: 3.490

7.  Dominant C-terminal deletions of FtsZ that affect its ability to localize in Caulobacter and its interaction with FtsA.

Authors:  N Din; E M Quardokus; M J Sackett; Y V Brun
Journal:  Mol Microbiol       Date:  1998-03       Impact factor: 3.501

8.  Colocalization of cell division proteins FtsZ and FtsA to cytoskeletal structures in living Escherichia coli cells by using green fluorescent protein.

Authors:  X Ma; D W Ehrhardt; W Margolin
Journal:  Proc Natl Acad Sci U S A       Date:  1996-11-12       Impact factor: 11.205

Review 9.  Morphogenesis of Escherichia coli.

Authors:  N Nanninga
Journal:  Microbiol Mol Biol Rev       Date:  1998-03       Impact factor: 11.056

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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  60 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.  Timing of FtsZ assembly in Escherichia coli.

Authors:  T Den Blaauwen; N Buddelmeijer; M E Aarsman; C M Hameete; N Nanninga
Journal:  J Bacteriol       Date:  1999-09       Impact factor: 3.490

3.  Green fluorescent protein functions as a reporter for protein localization in Escherichia coli.

Authors:  B J Feilmeier; G Iseminger; D Schroeder; H Webber; G J Phillips
Journal:  J Bacteriol       Date:  2000-07       Impact factor: 3.490

4.  Septal localization of the membrane-bound division proteins of Bacillus subtilis DivIB and DivIC is codependent only at high temperatures and requires FtsZ.

Authors:  V L Katis; R G Wake; E J Harry
Journal:  J Bacteriol       Date:  2000-06       Impact factor: 3.490

5.  Cell division in Escherichia coli: role of FtsL domains in septal localization, function, and oligomerization.

Authors:  J M Ghigo; J Beckwith
Journal:  J Bacteriol       Date:  2000-01       Impact factor: 3.490

6.  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

7.  Crystal structure of the cell division protein FtsA from Thermotoga maritima.

Authors:  F van den Ent; J Löwe
Journal:  EMBO J       Date:  2000-10-16       Impact factor: 11.598

Review 8.  Measurement of bacterial gene expression in vivo.

Authors:  I Hautefort; J C Hinton
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  2000-05-29       Impact factor: 6.237

9.  The Escherichia coli cell division protein FtsW is required to recruit its cognate transpeptidase, FtsI (PBP3), to the division site.

Authors:  Keri L N Mercer; David S Weiss
Journal:  J Bacteriol       Date:  2002-02       Impact factor: 3.490

10.  Analysis of ftsQ mutant alleles in Escherichia coli: complementation, septal localization, and recruitment of downstream cell division proteins.

Authors:  Joseph C Chen; Michael Minev; Jon Beckwith
Journal:  J Bacteriol       Date:  2002-02       Impact factor: 3.490

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