LytM-domain factors are required for daughter cell separation and rapid ampicillin-induced lysis in Escherichia coli.
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Peptidoglycan crosslinking relaxation promotes Helicobacter pylori's helical shape and stomach colonization.New insights into how Yersinia pestis adapts to its mammalian host during bubonic plagueStructure-function analysis of the LytM domain of EnvC, an activator of cell wall remodelling at theEscherichia colidivision siteA conformational switch controls cell wall-remodelling enzymes required for bacterial cell divisionThe crystal structure of the cell division amidase AmiC reveals the fold of the AMIN domain, a new peptidoglycan binding domainEnabling cell-cell communication via nanopore formation: structure, function and localization of the unique cell wall amidase AmiC2 of Nostoc punctiformeGenetic interaction maps in Escherichia coli reveal functional crosstalk among cell envelope biogenesis pathwaysLytM proteins play a crucial role in cell separation, outer membrane composition, and pathogenesis in nontypeable Haemophilus influenzae.The Bam machine: a molecular cooper.Genes required for and effects of alginate overproduction induced by growth of Pseudomonas aeruginosa on Pseudomonas isolation agar supplemented with ammonium metavanadate.Neisseria gonorrhoeae metalloprotease NGO1686 is required for full piliation, and piliation is required for resistance to H2O2- and neutrophil-mediated killingRapid beta-lactam-induced lysis requires successful assembly of the cell division machinery.A protein critical for cell constriction in the Gram-negative bacterium Caulobacter crescentus localizes at the division site through its peptidoglycan-binding LysM domains.DipM links peptidoglycan remodelling to outer membrane organization in Caulobacter.A highly coordinated cell wall degradation machine governs spore morphogenesis in Bacillus subtilis.DipM is required for peptidoglycan hydrolysis during chloroplast division.From the regulation of peptidoglycan synthesis to bacterial growth and morphology.Cheating by type 3 secretion system-negative Pseudomonas aeruginosa during pulmonary infection.Daughter cell separation is controlled by cytokinetic ring-activated cell wall hydrolysis.Studying a cell division amidase using defined peptidoglycan substrates.How antibiotics kill bacteria: from targets to networksSeptal and lateral wall localization of PBP5, the major D,D-carboxypeptidase of Escherichia coli, requires substrate recognition and membrane attachment.The β-lactam resistance protein Blr, a small membrane polypeptide, is a component of the Escherichia coli cell division machinery.A 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.Cell separation in Vibrio cholerae is mediated by a single amidase whose action is modulated by two nonredundant activatorsNucleoid occlusion factor SlmA is a DNA-activated FtsZ polymerization antagonist.Beta-lactam antibiotics induce a lethal malfunctioning of the bacterial cell wall synthesis machinery.DipM, a new factor required for peptidoglycan remodelling during cell division in Caulobacter crescentusIdentification of Escherichia coli ZapC (YcbW) as a component of the division apparatus that binds and bundles FtsZ polymersLipoprotein cofactors located in the outer membrane activate bacterial cell wall polymerases.A mutant Escherichia coli that attaches peptidoglycan to lipopolysaccharide and displays cell wall on its surface.A fail-safe mechanism in the septal ring assembly pathway generated by the sequential recruitment of cell separation amidases and their activators.Using superfolder green fluorescent protein for periplasmic protein localization studies.Screening and genetic characterization of thermo-tolerant Synechocystis sp. PCC6803 strains created by adaptive evolution.Heterogeneous bacterial persisters and engineering approaches to eliminate them.Essential PcsB putative peptidoglycan hydrolase interacts with the essential FtsXSpn cell division protein in Streptococcus pneumoniae D39.An ATP-binding cassette transporter-like complex governs cell-wall hydrolysis at the bacterial cytokinetic ring.Peptidoglycan hydrolases of Escherichia coli.Cytoplasmic Domain of MscS Interacts with Cell Division Protein FtsZ: A Possible Non-Channel Function of the Mechanosensitive Channel in Escherichia Coli.
P2860
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P2860
LytM-domain factors are required for daughter cell separation and rapid ampicillin-induced lysis in Escherichia coli.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
2009年论文
@zh
2009年论文
@zh-cn
name
LytM-domain factors are requir ...... ced lysis in Escherichia coli.
@en
type
label
LytM-domain factors are requir ...... ced lysis in Escherichia coli.
@en
prefLabel
LytM-domain factors are requir ...... ced lysis in Escherichia coli.
@en
P2860
P356
P1476
LytM-domain factors are requir ...... uced lysis in Escherichia coli
@en
P2093
Thomas G Bernhardt
P2860
P304
P356
10.1128/JB.00505-09
P577
2009-06-12T00:00:00Z