Murein (peptidoglycan) binding property of the essential cell division protein FtsN from Escherichia coli.
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Unstable Escherichia coli L forms revisited: growth requires peptidoglycan synthesisActivities and regulation of peptidoglycan synthasesNuclear Magnetic Resonance Solution Structure of the Peptidoglycan-Binding SPOR Domain from Escherichia coli DamX: Insights into Septal LocalizationOuter-membrane lipoprotein LpoB spans the periplasm to stimulate the peptidoglycan synthase PBP1BThe bacterial divisome: ready for its close-upCell age dependent concentration of Escherichia coli divisome proteins analyzed with ImageJ and ObjectJFunctional analysis of SleC from Clostridium difficile: an essential lytic transglycosylase involved in spore germinationThe periplasmic HrpB1 protein from Xanthomonas spp. binds to peptidoglycan and to components of the type III secretion system.A protein critical for cell constriction in the Gram-negative bacterium Caulobacter crescentus localizes at the division site through its peptidoglycan-binding LysM domains.Late assembly of the Vibrio cholerae cell division machinery postpones septation to the last 10% of the cell cycle.The C-terminal domain of Escherichia coli YfhD functions as a lytic transglycosylase.Discovery and characterization of three new Escherichia coli septal ring proteins that contain a SPOR domain: DamX, DedD, and RlpAFrom the regulation of peptidoglycan synthesis to bacterial growth and morphology.Identification and characterization of a gene cluster required for proper rod shape, cell division, and pathogenesis in Clostridium difficile.Daughter cell separation is controlled by cytokinetic ring-activated cell wall hydrolysis.The bacterial septal ring protein RlpA is a lytic transglycosylase that contributes to rod shape and daughter cell separation in Pseudomonas aeruginosaA role for the FtsQLB complex in cytokinetic ring activation revealed by an ftsL allele that accelerates divisionRoles for both FtsA and the FtsBLQ subcomplex in FtsN-stimulated cell constriction in Escherichia coli.The 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 ringBacterial growth and cell division: a mycobacterial perspective.DipM, a new factor required for peptidoglycan remodelling during cell division in Caulobacter crescentusA novel peptidoglycan binding protein crucial for PBP1A-mediated cell wall biogenesis in Vibrio cholerae.A fail-safe mechanism in the septal ring assembly pathway generated by the sequential recruitment of cell separation amidases and their activators.A DNA damage-induced, SOS-independent checkpoint regulates cell division in Caulobacter crescentus.Role for the nonessential N terminus of FtsN in divisome assemblyBacterial SPOR domains are recruited to septal peptidoglycan by binding to glycan strands that lack stem peptidesThe cell wall amidase AmiB is essential for Pseudomonas aeruginosa cell division, drug resistance and viability.Septum enlightenment: assembly of bacterial division proteins.An altered FtsA can compensate for the loss of essential cell division protein FtsN in Escherichia coliEvidence for functional overlap among multiple bacterial cell division proteins: compensating for the loss of FtsK.AMIN domains have a predicted role in localization of diverse periplasmic protein complexes.Structure-function analysis of the extracellular domain of the pneumococcal cell division site positioning protein MapZBacterial peptidoglycan (murein) hydrolases.Identification of SPOR domain amino acids important for septal localization, peptidoglycan binding, and a disulfide bond in the cell division protein FtsNAdvances in understanding E. coli cell fission.The physiology of bacterial cell division.Cell division in CorynebacterineaeStructural constraints and dynamics of bacterial cell wall architecture.Regulation of bacterial cell wall growth.The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain That Targets Proteins to the Site of Cell Division.
P2860
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P2860
Murein (peptidoglycan) binding property of the essential cell division protein FtsN from Escherichia coli.
description
2004 nî lūn-bûn
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2004年の論文
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2004年論文
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2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
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2004年論文
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2004年论文
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2004年论文
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name
Murein (peptidoglycan) binding ...... in FtsN from Escherichia coli.
@en
type
label
Murein (peptidoglycan) binding ...... in FtsN from Escherichia coli.
@en
prefLabel
Murein (peptidoglycan) binding ...... in FtsN from Escherichia coli.
@en
P2093
P2860
P1476
Murein (peptidoglycan) binding ...... in FtsN from Escherichia coli.
@en
P2093
Astrid Ursinus
Fusinita van den Ent
Joachim-Volker Höltje
Miguel de Pedro
Sonja Brechtel
P2860
P304
P356
10.1128/JB.186.20.6728-6737.2004
P577
2004-10-01T00:00:00Z