ZipA is a MAP-Tau homolog and is essential for structural integrity of the cytokinetic FtsZ ring during bacterial cell division.
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Cytokinesis in prokaryotes and eukaryotes: common principles and different solutionsCondensation of FtsZ filaments can drive bacterial cell division.The bacterial cytoskeletonSite-specific mutations of FtsZ--effects on GTPase and in vitro assemblyThe MAP2/Tau family of microtubule-associated proteinsThe bacterial cell-division protein ZipA and its interaction with an FtsZ fragment revealed by X-ray crystallographyKinetic modeling of the assembly, dynamic steady state, and contraction of the FtsZ ring in prokaryotic cytokinesisIdentification and characterization of a negative regulator of FtsZ ring formation in Bacillus subtilisLarge ring polymers align FtsZ polymers for normal septum formationPositive control of cell division: FtsZ is recruited by SsgB during sporulation of StreptomycesFtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one.Polymerization of Ftsz, a bacterial homolog of tubulin. is assembly cooperative?Cytokinesis in bacteriaComparative bacterial proteomics: analysis of the core genome concept.The MinC component of the division site selection system in Escherichia coli interacts with FtsZ to prevent polymerization.The polymerization mechanism of the bacterial cell division protein FtsZ.Assembly dynamics of the bacterial cell division protein FTSZ: poised at the edge of stabilityGenetic and functional analyses of the conserved C-terminal core domain of Escherichia coli FtsZDeletion of the min operon results in increased thermosensitivity of an ftsZ84 mutant and abnormal FtsZ ring assembly, placement, and disassembly.Cell division in Bacillus subtilis: FtsZ and FtsA association is Z-ring independent, and FtsA is required for efficient midcell Z-Ring assembly.Unique and overlapping roles for ZipA and FtsA in septal ring assembly in Escherichia coli.ZipA binds to FtsZ with high affinity and enhances the stability of FtsZ protofilaments.Imaging-based identification of a critical regulator of FtsZ protofilament curvature in Caulobacter.A gain-of-function mutation in ftsA bypasses the requirement for the essential cell division gene zipA in Escherichia coliConcentration and assembly of the division ring proteins FtsZ, FtsA, and ZipA during the Escherichia coli cell cycleThe early divisome protein FtsA interacts directly through its 1c subdomain with the cytoplasmic domain of the late divisome protein FtsN.Structural evidence that the P/Q domain of ZipA is an unstructured, flexible tether between the membrane and the C-terminal FtsZ-binding domain.Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA.A thermosensitive defect in the ATP binding pocket of FtsA can be suppressed by allosteric changes in the dimer interface.FtsZ and the division of prokaryotic cells and organelles.Glutamate 83 and arginine 85 of helix H3 bend are key residues for FtsZ polymerization, GTPase activity and cellular viability of Escherichia coli: lateral mutations affect FtsZ polymerization and E. coli viability.Bacterial growth and cell division: a mycobacterial perspective.Identification of Escherichia coli ZapC (YcbW) as a component of the division apparatus that binds and bundles FtsZ polymersAdenine nucleotide-dependent regulation of assembly of bacterial tubulin-like FtsZ by a hypermorph of bacterial actin-like FtsA.Oligomerization of FtsZ converts the FtsZ tail motif (conserved carboxy-terminal peptide) into a multivalent ligand with high avidity for partners ZipA and SlmA.Evidence for polar positional information independent of cell division and nucleoid occlusion.Interaction between cell division proteins FtsE and FtsZ.Extreme C terminus of bacterial cytoskeletal protein FtsZ plays fundamental role in assembly independent of modulatory proteins.A novel membrane-bound toxin for cell division, CptA (YgfX), inhibits polymerization of cytoskeleton proteins, FtsZ and MreB, in Escherichia coli.Expression, purification and crystallization of the cell-division protein YgfE from Escherichia coli.
P2860
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P2860
ZipA is a MAP-Tau homolog and is essential for structural integrity of the cytokinetic FtsZ ring during bacterial cell division.
description
1999 nî lūn-bûn
@nan
1999 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
ZipA is a MAP-Tau homolog and ...... uring bacterial cell division.
@ast
ZipA is a MAP-Tau homolog and ...... uring bacterial cell division.
@en
type
label
ZipA is a MAP-Tau homolog and ...... uring bacterial cell division.
@ast
ZipA is a MAP-Tau homolog and ...... uring bacterial cell division.
@en
prefLabel
ZipA is a MAP-Tau homolog and ...... uring bacterial cell division.
@ast
ZipA is a MAP-Tau homolog and ...... uring bacterial cell division.
@en
P2860
P356
P1433
P1476
ZipA is a MAP-Tau homolog and ...... uring bacterial cell division.
@en
P2093
D RayChaudhuri
P2860
P304
P356
10.1093/EMBOJ/18.9.2372
P407
P577
1999-05-01T00:00:00Z