Literature DB >> 9723913

FtsK is an essential cell division protein that is localized to the septum and induced as part of the SOS response.

L Wang1, J Lutkenhaus.   

Abstract

The role of ftsK in the growth of Escherichia coli was examined by turning off its expression. This resulted in smooth filaments without constrictions, indicating that FtsK was required at an early step in septation. Consistent with this, FtsK was found to localize to the septum in 70% of the cells, indicating that it was recruited relatively early in this process. FtsK localization required the function of FtsZ and FtsA but not FtsI and FtsQ. Consistent with this, Z rings were present in FtsK-depleted filaments. Subcellular localization of FtsK confirmed that it was a membrane protein. Only the first 202 amino acids of FtsK were essential for its role in membrane localization, cell division and viability. The expression of ftsK increased as part of the SOS response, and increased expression of ftsK conferred increased resistance to DNA damage.

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Year:  1998        PMID: 9723913     DOI: 10.1046/j.1365-2958.1998.00958.x

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


  72 in total

1.  An in vivo membrane fusion assay implicates SpoIIIE in the final stages of engulfment during Bacillus subtilis sporulation.

Authors:  M D Sharp; K Pogliano
Journal:  Proc Natl Acad Sci U S A       Date:  1999-12-07       Impact factor: 11.205

2.  All major regions of FtsK are required for resolution of chromosome dimers.

Authors:  D S Boyle; D Grant; G C Draper; W D Donachie
Journal:  J Bacteriol       Date:  2000-07       Impact factor: 3.490

3.  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

4.  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

5.  Prophage lambda induces terminal recombination in Escherichia coli by inhibiting chromosome dimer resolution. An orientation-dependent cis-effect lending support to bipolarization of the terminus.

Authors:  J Corre; J Patte; J M Louarn
Journal:  Genetics       Date:  2000-01       Impact factor: 4.562

6.  FtsK functions in the processing of a Holliday junction intermediate during bacterial chromosome segregation.

Authors:  F X Barre; M Aroyo; S D Colloms; A Helfrich; F Cornet; D J Sherratt
Journal:  Genes Dev       Date:  2000-12-01       Impact factor: 11.361

7.  ZipA is a MAP-Tau homolog and is essential for structural integrity of the cytokinetic FtsZ ring during bacterial cell division.

Authors:  D RayChaudhuri
Journal:  EMBO J       Date:  1999-05-04       Impact factor: 11.598

8.  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

9.  Effects of mutations involving cell division, recombination, and chromosome dimer resolution on a priA2::kan mutant.

Authors:  J D McCool; S J Sandler
Journal:  Proc Natl Acad Sci U S A       Date:  2001-07-17       Impact factor: 11.205

10.  Unique and overlapping roles for ZipA and FtsA in septal ring assembly in Escherichia coli.

Authors:  Sebastien Pichoff; Joe Lutkenhaus
Journal:  EMBO J       Date:  2002-02-15       Impact factor: 11.598

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