Role of two essential domains of Escherichia coli FtsA in localization and progression of the division ring.
about
Structure of the PilM-PilN Inner Membrane Type IV Pilus Biogenesis Complex from Thermus thermophilusFtsA forms actin-like protofilaments.In the beginning, Escherichia coli assembled the proto-ring: an initial phase of divisionBacterial actin and tubulin homologs in cell growth and divisionA new FtsZ-interacting protein, YlmF, complements the activity of FtsA during progression of cell division in Bacillus subtilisTemperature-regulated formation of mycelial mat-like biofilms by Legionella pneumophila.Cell division in Bacillus subtilis: FtsZ and FtsA association is Z-ring independent, and FtsA is required for efficient midcell Z-Ring assembly.FtsA mutants impaired for self-interaction bypass ZipA suggesting a model in which FtsA's self-interaction competes with its ability to recruit downstream division proteins.The early divisome protein FtsA interacts directly through its 1c subdomain with the cytoplasmic domain of the late divisome protein FtsN.Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA.A thermosensitive defect in the ATP binding pocket of FtsA can be suppressed by allosteric changes in the dimer interface.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 ringAdenine nucleotide-dependent regulation of assembly of bacterial tubulin-like FtsZ by a hypermorph of bacterial actin-like FtsA.Dr-FtsA, an actin homologue in Deinococcus radiodurans differentially affects Dr-FtsZ and Ec-FtsZ functions in vitroMutants, suppressors, and wrinkled colonies: mutant alleles of the cell division gene ftsQ point to functional domains in FtsQ and a role for domain 1C of FtsA in divisome assembly.A mutation in Escherichia coli ftsZ bypasses the requirement for the essential division gene zipA and confers resistance to FtsZ assembly inhibitors by stabilizing protofilament bundlingSeptum enlightenment: assembly of bacterial division proteins.Compensation for the loss of the conserved membrane targeting sequence of FtsA provides new insights into its function.The ftsA* gain-of-function allele of Escherichia coli and its effects on the stability and dynamics of the Z ringDimerization or oligomerization of the actin-like FtsA protein enhances the integrity of the cytokinetic Z ring.Dimer dynamics and filament organization of the bacterial cell division protein FtsASplitsville: structural and functional insights into the dynamic bacterial Z ring.Bacterial cytokinesis: From Z ring to divisome.FtsZ ring stability: of bundles, tubules, crosslinks, and curves.From models to pathogens: how much have we learned about Streptococcus pneumoniae cell division?The keepers of the ring: regulators of FtsZ assembly.The Escherichia coli divisome: born to divide.An Escherichia coli expression model reveals the species-specific function of FtsA from Neisseria gonorrhoeae in cell division.Escherichia coli FtsA forms lipid-bound minirings that antagonize lateral interactions between FtsZ protofilaments.The hypermorph FtsA* protein has an in vivo role in relieving the Escherichia coli proto-ring block caused by excess ZapC.Roles of the essential protein FtsA in cell growth and division in Streptococcus pneumoniae.Key role of two terminal domains in the bidirectional polymerization of FtsA protein.Reconstitution and organization of Escherichia coli proto-ring elements (FtsZ and FtsA) inside giant unilamellar vesicles obtained from bacterial inner membranes.Role of the FtsA C terminus as a switch for polymerization and membrane association.Crystal structure of the Actinomadura R39 DD-peptidase reveals new domains in penicillin-binding proteins.Morphological responses of Legionella pneumophila biofilm to nanoparticle exposure.Last but not least: new insights into how FtsN triggers constriction during Escherichia coli cell division.Identification of a region of FtsA required for interaction with FtsZ.
P2860
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P2860
Role of two essential domains of Escherichia coli FtsA in localization and progression of the division ring.
description
2004 nî lūn-bûn
@nan
2004 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Role of two essential domains ...... gression of the division ring.
@ast
Role of two essential domains ...... gression of the division ring.
@en
Role of two essential domains ...... gression of the division ring.
@nl
type
label
Role of two essential domains ...... gression of the division ring.
@ast
Role of two essential domains ...... gression of the division ring.
@en
Role of two essential domains ...... gression of the division ring.
@nl
prefLabel
Role of two essential domains ...... gression of the division ring.
@ast
Role of two essential domains ...... gression of the division ring.
@en
Role of two essential domains ...... gression of the division ring.
@nl
P2860
P1476
Role of two essential domains ...... gression of the division ring.
@en
P2093
Marta García-Ovalle
Miguel Vicente
P2860
P304
P356
10.1111/J.1365-2958.2004.04245.X
P407
P577
2004-09-01T00:00:00Z