Two active-site tyrosyl residues of protein TrwC act sequentially at the origin of transfer during plasmid R388 conjugation.
about
Disrupting antibiotic resistance propagation by inhibiting the conjugative DNA relaxaseExamination of an inverted repeat within the F factor origin of transfer: context dependence of F TraI relaxase DNA specificity.The Structure of the Minimal Relaxase Domain of MobA at 2.1 Å ResolutionPlasmid replication initiator RepB forms a hexamer reminiscent of ring helicases and has mobile nuclease domainsThe mechanism and control of DNA transfer by the conjugative relaxase of resistance plasmid pCU1Design of Novel Relaxase Substrates Based on Rolling Circle Replicases for Bioconjugation to DNA NanostructuresConjugative transfer can be inhibited by blocking relaxase activity within recipient cells with intrabodies.Mobilization function of the pBHR1 plasmid, a derivative of the broad-host-range plasmid pBBR1Site-specific recombinase and integrase activities of a conjugative relaxase in recipient cells.Site-specific integration of foreign DNA into minimal bacterial and human target sequences mediated by a conjugative relaxase.Bacterial conjugation: a two-step mechanism for DNA transport.Tracking F plasmid TraI relaxase processing reactions provides insight into F plasmid transferTyrosine partners coordinate DNA nicking by the Salmonella typhimurium plasmid pCU1 relaxase enzyme.A high security double lock and key mechanism in HUH relaxases controls oriT-processing for plasmid conjugation.Transfer of R388 derivatives by a pathogenesis-associated type IV secretion system into both bacteria and human cells.Swapping single-stranded DNA sequence specificities of relaxases from conjugative plasmids F and R100Dynamics of the IncW genetic backbone imply general trends in conjugative plasmid evolution.A Functional oriT in the Ptw Plasmid of Burkholderia cenocepacia Can Be Recognized by the R388 Relaxase TrwC.Exposing plasmids as the Achilles' heel of drug-resistant bacteria.A novel relaxase homologue is involved in chromosomal DNA processing for type IV secretion in Neisseria gonorrhoeae.Catalytic domain of plasmid pAD1 relaxase TraX defines a group of relaxases related to restriction endonucleasesThe expanding bacterial type IV secretion lexicon.Replication and conjugative mobilization of broad host-range IncQ plasmids.MobA, the DNA strand transferase of plasmid R1162: the minimal domain required for DNA processing at the origin of transfer.The relaxase of the Rhizobium etli symbiotic plasmid shows nic site cis-acting preference.Functional properties and structural requirements of the plasmid pMV158-encoded MobM relaxase domain.TraA and its N-terminal relaxase domain of the Gram-positive plasmid pIP501 show specific oriT binding and behave as dimers in solution.Relaxase DNA binding and cleavage are two distinguishable steps in conjugative DNA processing that involve different sequence elements of the nic siteA translocation motif in relaxase TrwC specifically affects recruitment by its conjugative type IV secretion system.A bacterial TrwC relaxase domain contains a thermally stable alpha-helical core.Nuclear targeting of a bacterial integrase that mediates site-specific recombination between bacterial and human target sequencesIdentification of the origin of transfer (oriT) and a new gene required for mobilization of the SXT/R391 family of integrating conjugative elements.Origin and fate of the 3' ends of single-stranded DNA generated by conjugal transfer of plasmid R1162Analysis of DNA processing reactions in bacterial conjugation by using suicide oligonucleotides.TrwC-mediated site-specific recombination is controlled by host factors altering local DNA topology.Roles of active site residues and the HUH motif of the F plasmid TraI relaxase.Translocation through the conjugative Type 4 secretion system requires unfolding of its protein substrate.Concerted action of NIC relaxase and auxiliary protein MobC in RA3 plasmid conjugation.Exchange of functional domains between a bacterial conjugative relaxase and the integrase of the human adeno-associated virus
P2860
Q24674141-D6C66A4E-3153-49DE-9194-EDD3D9BD9C3CQ25255767-6983DF28-3A76-488A-AEB9-65F94B3217FAQ27640657-DC16735A-91A2-4556-BC1A-A540A8357685Q27655468-6FD3D7E7-390F-4986-BE19-A9E75789207EQ27661390-000D7A8D-4E4A-4AC4-ABF2-81315D18B5A7Q28551074-B8839EF7-95EB-41DC-9820-C006654AA660Q33266305-BF59CC63-ACD0-4D95-84EE-35634DB7EF20Q33995841-C44C778B-EEE2-4F63-AEA9-1E3300148CEEQ34132259-D37A9C80-5D08-4175-9A30-AA42495F24EDQ34146610-380F0A8D-97F6-42A8-A2AE-8439D6206B90Q34722956-07E2E888-900D-422E-8912-2C0161874EC4Q34779343-DE0D0E49-24EC-4632-9FCC-461097F3B907Q34905620-AD31C4A8-1525-4AA4-85FD-D6EF7E9D3231Q35225102-D38359E9-B839-4C52-B646-897918F5FC4DQ35530988-D882DA35-88E7-4B47-A04C-51CBB213F53FQ36160589-EF2E980F-9859-43EB-BBFD-9095AC5A1965Q36616678-C137E7DB-F2B4-4781-AB21-1370781E2AD4Q36859021-F9738EFB-1AE9-437F-A19E-B00581CB85D3Q36943396-9A7960DC-BF98-4613-B2C5-7C29727AE547Q36980934-4478AF8B-4BA5-4F26-B72F-DFE792BAF7F8Q37104094-5698E209-82E5-428D-92F5-A710F3E24E7CQ37275377-B31631A7-9063-4F98-8875-B73B0B283F67Q37493631-B40E4A2F-7108-4552-8986-85D32028F7C7Q38292165-26E3C5CA-ED12-4F8E-89C7-DFD0E7AE0884Q38310561-B803AE94-54A8-4B5A-A70A-8E84F12F0891Q38315967-FD2336BB-3AB5-4E71-8760-A31D36333E47Q38334075-E141FBE8-DC41-4496-A4B4-43FD644327C0Q38347343-D1C9F2DC-C287-4338-B965-FD1A9CF73726Q39101676-911FA849-933F-4762-A9EE-A4D7F6EF1198Q39787948-7A014192-9128-4BE9-B0E4-30C10F501CFDQ39822300-95B1D467-1C51-4B12-8F8A-9316931EC7E1Q41340424-93121471-1D36-4D8A-8FF2-E90A50CDC1AFQ42181543-5B3A855E-EA17-41D2-8597-C9E0E99A5678Q42411932-C22862E7-A0D2-4B82-ACFC-D538743A9209Q42633712-C7EC5576-EDE6-4F54-8311-FF40BE7FA42EQ46985714-CB84A700-E23D-4CEC-98D1-C609367CCBF8Q47222977-8A4FF6FA-EB1E-45C4-9E94-BD5892C235BEQ52873805-D149BE68-5CFE-4E26-8A07-39A664A2E285Q57753642-EE29899E-FD87-4958-A90F-990CAAC58305
P2860
Two active-site tyrosyl residues of protein TrwC act sequentially at the origin of transfer during plasmid R388 conjugation.
description
2000 nî lūn-bûn
@nan
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
2000年论文
@zh
2000年论文
@zh-cn
name
Two active-site tyrosyl residu ...... ring plasmid R388 conjugation.
@en
type
label
Two active-site tyrosyl residu ...... ring plasmid R388 conjugation.
@en
prefLabel
Two active-site tyrosyl residu ...... ring plasmid R388 conjugation.
@en
P2093
P356
P1476
Two active-site tyrosyl residu ...... ring plasmid R388 conjugation.
@en
P2093
P304
P356
10.1006/JMBI.1999.3425
P407
P577
2000-02-01T00:00:00Z