Literature DB >> 9282742

FtsN, a late recruit to the septum in Escherichia coli.

S G Addinall1, C Cao, J Lutkenhaus.   

Abstract

The localization of FtsN in Escherichia coli was inves tigated by immunofluorescence microscopy. FtsN is an essential cell division protein with a simple bitopic topology, a short N-terminal cytoplasmic segment fused to a large carboxy periplasmic domain through a single transmembrane domain. FtsN was found to localize to the septum in a ring pattern similar to that observed for FtsZ and FtsA, although the frequency of cells with rings was less. A MalG-FtsN fusion was also localized to the septum, indicating that the information for FtsN localization is supplied by its periplasmic domain. FtsN localization was dependent upon the prior localization of FtsZ and FtsA and required the function of FtsI and FtsQ. Consistent with FtsN functioning after FtsZ, Z rings were observed in a mutant depleted of FtsN.

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Year:  1997        PMID: 9282742     DOI: 10.1046/j.1365-2958.1997.4641833.x

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


  89 in total

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Authors:  V L Katis; R G Wake; E J Harry
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Authors:  J M Ghigo; J Beckwith
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Authors:  D RayChaudhuri
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8.  A vital stain for studying membrane dynamics in bacteria: a novel mechanism controlling septation during Bacillus subtilis sporulation.

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Journal:  Mol Microbiol       Date:  1999-02       Impact factor: 3.501

9.  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
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10.  Crystal structure of the cell division protein FtsA from Thermotoga maritima.

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Journal:  EMBO J       Date:  2000-10-16       Impact factor: 11.598

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