A fail-safe mechanism in the septal ring assembly pathway generated by the sequential recruitment of cell separation amidases and their activators.
about
A 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 domainIn the beginning, Escherichia coli assembled the proto-ring: an initial phase of divisionAn Amidase_3 domain-containing N-acetylmuramyl-L-alanine amidase is required for mycobacterial cell division.DipM is required for peptidoglycan hydrolysis during chloroplast division.From the regulation of peptidoglycan synthesis to bacterial growth and morphology.Peptidoglycan synthesis machinery in Agrobacterium tumefaciens during unipolar growth and cell division.The bacterial septal ring protein RlpA is a lytic transglycosylase that contributes to rod shape and daughter cell separation in Pseudomonas aeruginosaThe early divisome protein FtsA interacts directly through its 1c subdomain with the cytoplasmic domain of the late divisome protein FtsN.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.FtsEX acts on FtsA to regulate divisome assembly and activity.Cell separation in Vibrio cholerae is mediated by a single amidase whose action is modulated by two nonredundant activatorsGenes required for growth at high hydrostatic pressure in Escherichia coli K-12 identified by genome-wide screening.Sublethal concentrations of carbapenems alter cell morphology and genomic expression of Klebsiella pneumoniae biofilmsUsing superfolder green fluorescent protein for periplasmic protein localization studies.A DNA damage-induced, SOS-independent checkpoint regulates cell division in Caulobacter crescentus.Endopeptidase-mediated beta lactam tolerance.Escherichia coli low-molecular-weight penicillin-binding proteins help orient septal FtsZ, and their absence leads to asymmetric cell division and branching.More than just lysins: peptidoglycan hydrolases tailor the cell wallBacterial 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.Defining the rate-limiting processes of bacterial cytokinesisAmidase Activity of AmiC Controls Cell Separation and Stem Peptide Release and Is Enhanced by NlpD in Neisseria gonorrhoeae.Twin-arginine translocation system (tat) mutants of Salmonella are attenuated due to envelope defects, not respiratory defectsIdentification of SPOR domain amino acids important for septal localization, peptidoglycan binding, and a disulfide bond in the cell division protein FtsNDynamic protein complexes for cell growthCytoskeletal proteins of actinobacteria.Bacterial cytokinesis: From Z ring to divisome.The physiology of bacterial cell division.Engineered fluorescent proteins illuminate the bacterial periplasmThe Type IVa Pilus Machinery Is Recruited to Sites of Future Cell DivisionThe SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain That Targets Proteins to the Site of Cell Division.The Escherichia coli divisome: born to divide.ClpXP and ClpAP control the Escherichia coli division protein ZapC by proteolysis.Influence of FtsZ GTPase activity and concentration on nanoscale Z-ring structure in vivo revealed by three-dimensional Superresolution imaging.NlpD links cell wall remodeling and outer membrane invagination during cytokinesis in Escherichia coli.A role for FtsA in SPOR-independent localization of the essential Escherichia coli cell division protein FtsN.Substrate specificity of an elongation-specific peptidoglycan endopeptidase and its implications for cell wall architecture and growth of Vibrio cholerae
P2860
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P2860
A fail-safe mechanism in the septal ring assembly pathway generated by the sequential recruitment of cell separation amidases and their activators.
description
2011 nî lūn-bûn
@nan
2011 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
A fail-safe mechanism in the s ...... amidases and their activators.
@ast
A fail-safe mechanism in the s ...... amidases and their activators.
@en
type
label
A fail-safe mechanism in the s ...... amidases and their activators.
@ast
A fail-safe mechanism in the s ...... amidases and their activators.
@en
prefLabel
A fail-safe mechanism in the s ...... amidases and their activators.
@ast
A fail-safe mechanism in the s ...... amidases and their activators.
@en
P2093
P2860
P356
P1476
A fail-safe mechanism in the s ...... amidases and their activators.
@en
P2093
Nick T Peters
Thomas G Bernhardt
P2860
P304
P356
10.1128/JB.00316-11
P407
P577
2011-07-15T00:00:00Z