Dimerization or oligomerization of the actin-like FtsA protein enhances the integrity of the cytokinetic Z ring.
about
Bacterial actins and their diversityStructural Organization of FtsB, a Transmembrane Protein of the Bacterial DivisomeFtsA 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 divisionAlp7R regulates expression of the actin-like protein Alp7A in Bacillus subtilisFtsA 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.Isolation, characterization and lipid-binding properties of the recalcitrant FtsA division protein from Escherichia coli.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 ringIdentification of Escherichia coli ZapC (YcbW) as a component of the division apparatus that binds and bundles FtsZ polymersAdenine nucleotide-dependent regulation of assembly of bacterial tubulin-like FtsZ by a hypermorph of bacterial actin-like FtsA.The Kil peptide of bacteriophage λ blocks Escherichia coli cytokinesis via ZipA-dependent inhibition of FtsZ assemblyA mutation in Escherichia coli ftsZ bypasses the requirement for the essential division gene zipA and confers resistance to FtsZ assembly inhibitors by stabilizing protofilament bundlingCompensation for the loss of the conserved membrane targeting sequence of FtsA provides new insights into its function.Dimer dynamics and filament organization of the bacterial cell division protein FtsAA mutation in the promoter region of zipA, a component of the divisome, suppresses the shape defect of RodZ-deficient cells.Splitsville: 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.Roles of pneumococcal DivIB in cell divisionA role for FtsA in SPOR-independent localization of the essential Escherichia coli cell division protein FtsN.A bacterial actin unites to divide bacterial cells.Key role of two terminal domains in the bidirectional polymerization of FtsA protein.Phylogenetic analysis identifies many uncharacterized actin-like proteins (Alps) in bacteria: regulated polymerization, dynamic instability and treadmilling in Alp7A.Role of the FtsA C terminus as a switch for polymerization and membrane association.A 1 MDa protein complex containing critical components of the Escherichia coli divisome.Escherichia coli ZipA Organizes FtsZ Polymers into Dynamic Ring-Like Protofilament Structures.
P2860
Q27001005-720AB5B9-A69B-402A-B612-194CEB5703FDQ27676985-31D5DDFA-5C58-43D9-A595-6EE315029468Q27678310-8BACDACA-9EF9-46F5-AC96-745E48DD981CQ27694716-C709060A-D755-473C-9AD4-8127D6B7B315Q28083563-CBA2124E-8FA7-42A8-A55C-614B51318911Q30513984-17FD6911-C11F-4573-A16E-8E96B7BDB50AQ34235469-0C082EE9-1462-4380-B962-1C31526262D7Q34253906-F066328E-E9C1-4FE2-978D-3ECCC568DFC6Q34326565-980DB06E-FE71-49C9-AF6E-513CAB712197Q34438104-51E24C05-39E2-447E-9611-168ED094B543Q34453157-BD4ED920-0A06-431E-A660-84990D4B459DQ34740554-3302CC8B-9D58-4DCC-B603-012793E14077Q34964917-BA283935-2794-4167-80F3-E78E63A8B7FAQ35126034-457FFA86-E347-4E09-A63C-D226DF1463C1Q36271359-3BD5BFAC-7FCA-4455-98A0-EC85C7FF0ABEQ36345584-E256E035-E20C-44D3-A56C-F5F007190822Q37283629-0B3286B5-9A79-46BD-8E45-59033E2751E0Q37318699-109154F0-8FA0-4581-8BC5-CB92E5F92D58Q37623180-0218E3AF-636D-4C3A-8CA0-0E6717786A61Q38034197-35A0C6E2-CAB5-464C-A944-0C59DA467541Q38086221-E896C51B-21B1-4A71-9EF1-CD4396B16D5CQ39759327-288D6F85-2B09-412B-8BEC-6F09DEED6D37Q42115316-0AD657B7-5A68-43C3-BA7E-FBA554BE8A84Q42182204-0C41CD1F-A339-4994-84F0-1FA37BAF8E85Q42605167-435306E1-4374-4261-8E16-5867B8A2550CQ42926353-9888FA11-4924-4C48-83B2-33721F031448Q43050685-2834F195-35C6-4C81-B236-1D4483CEFD0DQ43140492-BD8313DF-8F14-45A7-A0A8-F6E36C096D68Q55314599-EBF2C7EE-5712-4C5A-A414-A2BC171D1D32
P2860
Dimerization or oligomerization of the actin-like FtsA protein enhances the integrity of the cytokinetic Z ring.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Dimerization or oligomerizatio ...... ity of the cytokinetic Z ring.
@ast
Dimerization or oligomerizatio ...... ity of the cytokinetic Z ring.
@en
type
label
Dimerization or oligomerizatio ...... ity of the cytokinetic Z ring.
@ast
Dimerization or oligomerizatio ...... ity of the cytokinetic Z ring.
@en
prefLabel
Dimerization or oligomerizatio ...... ity of the cytokinetic Z ring.
@ast
Dimerization or oligomerizatio ...... ity of the cytokinetic Z ring.
@en
P2860
P1476
Dimerization or oligomerizatio ...... rity of the cytokinetic Z ring
@en
P2093
William Margolin
P2860
P304
P356
10.1111/J.1365-2958.2007.05998.X
P407
P577
2007-11-06T00:00:00Z