The conserved C-terminal tail of FtsZ is required for the septal localization and division inhibitory activity of MinC(C)/MinD.
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The Min system and other nucleoid-independent regulators of Z ring positioningThe Nucleoid Occlusion SlmA Protein Accelerates the Disassembly of the FtsZ Protein Polymers without Affecting Their GTPase ActivityFtsZ placement in nucleoid-free bacteriaThe MinCDJ system in Bacillus subtilis prevents minicell formation by promoting divisome disassemblyDetermination of the structure of the MinD-ATP complex reveals the orientation of MinD on the membrane and the relative location of the binding sites for MinE and MinCFtsA forms actin-like protofilaments.Crystal structure of the N-terminal domain of MinC dimerized via domain swappingIn the beginning, Escherichia coli assembled the proto-ring: an initial phase of divisionGenetic and biochemical characterization of the MinC-FtsZ interaction in Bacillus subtilisA flexible C-terminal linker is required for proper FtsZ assembly in vitro and cytokinetic ring formation in vivoProteolysis-Dependent Remodeling of the Tubulin Homolog FtsZ at the Division Septum in Escherichia coli.Changes in the Min oscillation pattern before and after cell birthFtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one.MinCDE exploits the dynamic nature of FtsZ filaments for its spatial regulationAsymmetric constriction of dividing Escherichia coli cells induced by expression of a fusion between two min proteins.Genome-scale analysis and comparison of gene expression profiles in developing and germinated pollen in Oryza sativa.Characterization of ftsZ mutations that render Bacillus subtilis resistant to MinCEssential biological processes of an emerging pathogen: DNA replication, transcription, and cell division in Acinetobacter sppBacillus subtilis SepF binds to the C-terminus of FtsZ.A thermosensitive defect in the ATP binding pocket of FtsA can be suppressed by allosteric changes in the dimer interface.Reconstitution of self-organizing protein gradients as spatial cues in cell-free systemsThe bypass of ZipA by overexpression of FtsN requires a previously unknown conserved FtsN motif essential for FtsA-FtsN interaction supporting a model in which FtsA monomers recruit late cell division proteins to the Z ringDifferences in MinC/MinD sensitivity between polar and internal Z rings in Escherichia coli.Location of dual sites in E. coli FtsZ important for degradation by ClpXP; one at the C-terminus and one in the disordered linker.Oligomerization of FtsZ converts the FtsZ tail motif (conserved carboxy-terminal peptide) into a multivalent ligand with high avidity for partners ZipA and SlmA.SlmA antagonism of FtsZ assembly employs a two-pronged mechanism like MinCD.Extreme C terminus of bacterial cytoskeletal protein FtsZ plays fundamental role in assembly independent of modulatory proteins.Characterization of the FtsZ C-Terminal Variable (CTV) Region in Z-Ring Assembly and Interaction with the Z-Ring Stabilizer ZapD in E. coli CytokinesisA mutation in Escherichia coli ftsZ bypasses the requirement for the essential division gene zipA and confers resistance to FtsZ assembly inhibitors by stabilizing protofilament bundlingA specific role for the ZipA protein in cell division: stabilization of the FtsZ protein.Efficient Multiscale Models of Polymer AssemblyCharacterization of DicB by partially masking its potent inhibitory activity of cell division.Splitsville: structural and functional insights into the dynamic bacterial Z ring.Advances in understanding E. coli cell fission.Bacterial cytokinesis: From Z ring to divisome.Functional analysis of the cyclophilin PpiB role in bacterial cell division.FtsZ-ring Architecture and Its Control by MinCD.Multi-color imaging of the bacterial nucleoid and division proteins with blue, orange, and near-infrared fluorescent proteins.ClpXP and ClpAP control the Escherichia coli division protein ZapC by proteolysis.Crystal structure of the Z-ring associated cell division protein ZapC from Escherichia coli.
P2860
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P2860
The conserved C-terminal tail of FtsZ is required for the septal localization and division inhibitory activity of MinC(C)/MinD.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on April 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
The conserved C-terminal tail ...... on inhibitory activity of MinC
@nl
The conserved C-terminal tail ...... tory activity of MinC(C)/MinD.
@en
type
label
The conserved C-terminal tail ...... on inhibitory activity of MinC
@nl
The conserved C-terminal tail ...... tory activity of MinC(C)/MinD.
@en
prefLabel
The conserved C-terminal tail ...... on inhibitory activity of MinC
@nl
The conserved C-terminal tail ...... tory activity of MinC(C)/MinD.
@en
P2860
P1476
The conserved C-terminal tail ...... tory activity of MinC(C)/MinD.
@en
P2093
Joe Lutkenhaus
P2860
P304
P356
10.1111/J.1365-2958.2009.06651.X
P407
P577
2009-04-01T00:00:00Z