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Article

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

Molecular microbiology - 1 Feb 2006

Hamoen Leendert W, Meile Jean-Christophe, de Jong Wouter, Noirot Philippe, Errington Jeff

Abstract excerpt

Cell division in nearly all bacteria is initiated by polymerization of the conserved tubulin-like protein FtsZ into a ring-like structure at midcell. This Z-ring functions as a scaffold for a group of conserved proteins that execute the synthesis of the division septum (the divisome). Here we describe the identification of a new cell division protein in Bacillus subtilis. This protein is conserved in Gram...

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Identifiers

PMID: 16420366
DOI: 10.1111/j.1365-2958.2005.04987.x

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

SepF, a novel FtsZ-interacting protein required for a late step in cell division.PMID 16420366Read ↗

Bacillus subtilis SepF binds to the C-terminus of FtsZ.Semantic proximity Read ↗

Cytological characterization of YpsB, a novel component of the Bacillus subtilis divisome.Semantic proximity Read ↗

SepG coordinates sporulation-specific cell division and nucleoid organization in Streptomyces coelicolor.Semantic proximity Read ↗

Defining the order of assembly of the <i>Clostridioides difficile</i> divisome complexSemantic proximity Read ↗

Direct interaction of FtsZ and MreB is required for septum synthesis and cell division in Escherichia coli.Semantic proximity Read ↗

Roles of the Essential Protein FtsA in Cell Growth and Division in Streptococcus pneumoniaeSemantic proximity Read ↗

RefZ facilitates the switch from medial to polar division during spore formation in Bacillus subtilis.Semantic proximity Read ↗

Structural and mutational analysis of the cell division protein FtsQ.Semantic proximity Read ↗

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

A role for the FtsQLB complex in cytokinetic ring activation revealed by an ftsL allele that accelerates division.Semantic proximity Read ↗

Structure and Mutational Analyses of Escherichia coli ZapD Reveal Charged Residues Involved in FtsZ Filament Bundling.Semantic proximity Read ↗

The Division Defect of a Bacillus subtilis minD noc Double Mutant Can Be Suppressed by Spx-Dependent and Spx-Independent Mechanisms.Semantic proximity Read ↗

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