SlmA antagonism of FtsZ assembly employs a two-pronged mechanism like MinCD.
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The Nucleoid Occlusion SlmA Protein Accelerates the Disassembly of the FtsZ Protein Polymers without Affecting Their GTPase ActivityBacterial actin and tubulin homologs in cell growth and divisionThe 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 ringOligomerization of FtsZ converts the FtsZ tail motif (conserved carboxy-terminal peptide) into a multivalent ligand with high avidity for partners ZipA and SlmA.Evidence That Bacteriophage λ Kil Peptide Inhibits Bacterial Cell Division by Disrupting FtsZ Protofilaments and Sequestering Protein Subunits.Characterization of the FtsZ C-Terminal Variable (CTV) Region in Z-Ring Assembly and Interaction with the Z-Ring Stabilizer ZapD in E. coli CytokinesisEfficient Multiscale Models of Polymer AssemblyStructures of the nucleoid occlusion protein SlmA bound to DNA and the C-terminal domain of the cytoskeletal protein FtsZ.Cell cycle regulation by the bacterial nucleoid.Guiding divisome assembly and controlling its activity.Spatial coordination between chromosomes and cell division proteins in Escherichia coli.How much territory can a single E. coli cell control?The keepers of the ring: regulators of FtsZ assembly.Functional analysis of the cyclophilin PpiB role in bacterial cell division.ZapA and ZapB form an FtsZ-independent structure at midcell.Bacterial Nucleoid Occlusion: Multiple Mechanisms for Preventing Chromosome Bisection During Cell Division.Multi-color imaging of the bacterial nucleoid and division proteins with blue, orange, and near-infrared fluorescent proteins.The nucleoid occlusion factor Noc controls DNA replication initiation in Staphylococcus aureus.A benzamide-dependent ftsZ mutant reveals residues crucial for Z-ring assembly.The essential role of SepF in mycobacterial division.MinC/MinD copolymers are not required for Min function.CbtA toxin of Escherichia coli inhibits cell division and cell elongation via direct and independent interactions with FtsZ and MreBNucleoid occlusion protein Noc recruits DNA to the bacterial cell membrane.The N-succinyl-l,l-diaminopimelic acid desuccinylase DapE acts through ZapB to promote septum formation in Escherichia coli.MinC and FtsZ mutant analysis provides insight into MinC/MinD-mediated Z Ring disassembly.Subcellular Organization: A Critical Feature of Bacterial Cell Replication.Beyond force generation: Why is a dynamic ring of FtsZ polymers essential for bacterial cytokinesis?Unite to divide: Oligomerization of tubulin and actin homologs regulates initiation of bacterial cell division.Absence of the Min System Does Not Cause Major Cell Division Defects in Agrobacterium tumefaciens.
P2860
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P2860
SlmA antagonism of FtsZ assembly employs a two-pronged mechanism like MinCD.
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2014 nî lūn-bûn
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2014 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի հուլիսին հրատարակված գիտական հոդված
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2014年の論文
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2014年論文
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2014年論文
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2014年論文
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2014年論文
@zh-mo
2014年論文
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2014年论文
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name
SlmA antagonism of FtsZ assembly employs a two-pronged mechanism like MinCD.
@ast
SlmA antagonism of FtsZ assembly employs a two-pronged mechanism like MinCD.
@en
type
label
SlmA antagonism of FtsZ assembly employs a two-pronged mechanism like MinCD.
@ast
SlmA antagonism of FtsZ assembly employs a two-pronged mechanism like MinCD.
@en
prefLabel
SlmA antagonism of FtsZ assembly employs a two-pronged mechanism like MinCD.
@ast
SlmA antagonism of FtsZ assembly employs a two-pronged mechanism like MinCD.
@en
P2860
P1433
P1476
SlmA antagonism of FtsZ assembly employs a two-pronged mechanism like MinCD.
@en
P2093
Joe Lutkenhaus
Shishen Du
P2860
P304
P356
10.1371/JOURNAL.PGEN.1004460
P577
2014-07-31T00:00:00Z