SepF increases the assembly and bundling of FtsZ polymers and stabilizes FtsZ protofilaments by binding along its length.
about
The MinCDJ system in Bacillus subtilis prevents minicell formation by promoting divisome disassemblyStructural and genetic analyses reveal the protein SepF as a new membrane anchor for the Z ringBacterial actin and tubulin homologs in cell growth and divisionGenetic and biochemical characterization of the MinC-FtsZ interaction in Bacillus subtilisLarge ring polymers align FtsZ polymers for normal septum formationFtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one.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.FtsA mutants impaired for self-interaction bypass ZipA suggesting a model in which FtsA's self-interaction competes with its ability to recruit downstream division proteins.Bacillus subtilis SepF binds to the C-terminus of FtsZ.Discovery of anti-TB agents that target the cell-division protein FtsZ.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.Identification of Escherichia coli ZapC (YcbW) as a component of the division apparatus that binds and bundles FtsZ polymersOligomerization of FtsZ converts the FtsZ tail motif (conserved carboxy-terminal peptide) into a multivalent ligand with high avidity for partners ZipA and SlmA.Tetracycline hypersensitivity of an ezrA mutant links GalE and TseB (YpmB) to cell divisionZipA is required for FtsZ-dependent preseptal peptidoglycan synthesis prior to invagination during cell division.A specific role for the ZipA protein in cell division: stabilization of the FtsZ protein.The conserved DNA-binding protein WhiA is involved in cell division in Bacillus subtilis.Targeting FtsZ for antibacterial therapy: a promising avenue.Bacterial cytokinesis: From Z ring to divisome.The structure, function, and regulation of Mycobacterium FtsZ.The physiology of bacterial cell division.The keepers of the ring: regulators of FtsZ assembly.FtsZ polymerization assays: simple protocols and considerations.Identification of agents targeting FtsZ assembly.Prokaryotic cytokinesis: little rings bring big cylindrical things.The essential role of SepF in mycobacterial division.Characterization of the FtsZ-interacting septal proteins SepF and Ftn6 in the spherical-celled cyanobacterium Synechocystis strain PCC 6803.Bacterial cytokinesis: FzlA frizzes FtsZ filaments for fission force.Promoting assembly and bundling of FtsZ as a strategy to inhibit bacterial cell division: a new approach for developing novel antibacterial drugs.Lateral FtsZ association and the assembly of the cytokinetic Z ring in bacteria.An essential cell division protein directly regulates FtsZ dynamicsFtsZ of Filamentous, Heterocyst-Forming Cyanobacteria Has a Conserved N-Terminal Peptide Required for Normal FtsZ Polymerization and Cell Division
P2860
Q27332189-797079E6-BB67-4E8C-8636-D55E3E3FBE11Q27680581-8796730A-CEF1-4266-9265-E15649AA47BAQ28083563-148F3130-105F-4218-BA91-8921E94EA701Q28486034-4A2F8F97-95A9-486A-A105-8C1F3C4AC294Q28489014-3D0615F6-D8D5-4D5E-A681-D79932D8E8A4Q30497729-003D71F6-68CB-48A3-A939-6B0186F1BF49Q34099117-41AD429D-574F-4275-AC09-D1E9B5CDE25BQ34155531-6BB5899A-6A59-4124-86D8-986C94171F50Q34235469-B3B63740-6D32-4CD2-BBEA-0C32F8714F00Q34389510-72D2B4B7-25EF-46C2-86F8-C7E07453EB70Q34576179-CDE081B1-9468-49AF-AB0D-ABB33DF7B10CQ34577628-F66478B5-CF04-42EB-8EF4-C5D6FC403B65Q34740554-1B2EAB1A-C178-4970-8EF0-0A5B87280550Q35190227-6DE84F17-4A66-490F-BAFA-23DE47C912BCQ35624971-178672AB-AFA4-4F93-8FB5-C76AB342F508Q36276314-17E101B5-3912-4D91-9260-A78C67D23826Q36579510-EEC0594A-6F1C-4ADE-8190-764A31E56A42Q37469743-FB1296E3-1001-410F-AC64-614E4022A889Q37573808-AA5A8414-0107-4027-9EC2-D7999ED3D814Q38034197-AA7F9D24-3C07-4F87-B51E-D2B4067912D2Q38039001-51A5EF74-318C-4737-8B3B-128361D80270Q38065215-40F99192-C2B8-4E6A-8CC0-7A618081DACEQ38588069-35D2BC8F-CD7C-46CD-8719-34152D94DE16Q38823070-5A918BD4-DDF6-4775-B2BC-4193FA78EC5EQ38855290-B89219DC-1C0E-4405-AAA2-42560A18E158Q38876380-151600FE-7183-42B2-A3AD-66F4E3C53117Q40974615-6D1249E9-A860-4D20-BB42-04A4728197A7Q41810422-062BD4CE-B692-4345-881A-FC692492085EQ42131506-A57BD2F6-E825-4EE4-9A06-F630EE792D4DQ45937068-60785F80-AB78-4B22-B757-0D8BBBE86FDCQ53364709-77A057B9-8A0E-4E24-A681-6F81542472B1Q57045692-4A2C583F-D0E5-442F-8257-90F93CFD5BD6Q58586630-351A753A-38B9-4D26-AC09-97A61C48010D
P2860
SepF increases the assembly and bundling of FtsZ polymers and stabilizes FtsZ protofilaments by binding along its length.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
SepF increases the assembly an ...... s by binding along its length.
@en
SepF increases the assembly an ...... s by binding along its length.
@nl
type
label
SepF increases the assembly an ...... s by binding along its length.
@en
SepF increases the assembly an ...... s by binding along its length.
@nl
prefLabel
SepF increases the assembly an ...... s by binding along its length.
@en
SepF increases the assembly an ...... s by binding along its length.
@nl
P2093
P2860
P356
P1476
SepF increases the assembly an ...... s by binding along its length.
@en
P2093
Dulal Panda
Jay Kumar Singh
Ravindra D Makde
Vinay Kumar
P2860
P304
31116-31124
P356
10.1074/JBC.M805910200
P407
P577
2008-09-09T00:00:00Z