About: Evidence that DNA helicase I and oriT site-specific nicking are both functions of the F TraI protein

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About: Evidence that DNA helicase I and oriT site-specific nicking are both functions of the F TraI protein Goto Sponge Distinct Permalink

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scientific article published on 01 November 1988

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в листопаді 1988 (uk) im November 1988 veröffentlichter wissenschaftlicher Artikel (de) scientific article published on 01 November 1988 (en) artículu científicu espublizáu en payares de 1988 (ast)
publication date	wds:Q69847405-2A60ED35-42E6-42BB-ADC1-4E8327EBFA13
publication date	1988-11-01 00:00:00Z (xsd:dateTime)
author name string	wds:Q69847405-072B8123-90E7-4E48-B0F7-EE0A7ACF3A4C wds:Q69847405-89D580E1-1B88-4302-B13E-E17B90E51E06
author name string	B A Traxler E G Minkley
rdfs:label	Evidence that DNA helicase I and oriT site-specific nicking are both functions of the F TraI protein (en) Evidence that DNA helicase I and oriT site-specific nicking are both functions of the F TraI protein (nl)
skos:prefLabel	Evidence that DNA helicase I and oriT site-specific nicking are both functions of the F TraI protein (en) Evidence that DNA helicase I and oriT site-specific nicking are both functions of the F TraI protein (nl)
name	Evidence that DNA helicase I and oriT site-specific nicking are both functions of the F TraI protein (en) Evidence that DNA helicase I and oriT site-specific nicking are both functions of the F TraI protein (nl)
title	wds:Q69847405-10BA9F82-A9DE-4D06-8D44-BB091E1CB1F2
title	Evidence that DNA helicase I and oriT site-specific nicking are both functions of the F TraI protein (en)
page(s)	wds:Q69847405-2982616A-2933-4DBC-9E51-8262395D7A5A
page(s)	205-209
instance of	wds:Q69847405-8FEDA6C8-28EC-45B3-887E-FE3E337B8A06
instance of	scholarly article
PubMed ID	wds:Q69847405-B07FA012-E726-47D1-805C-81C67B0B81E8
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/2851049
PubMed ID	2851049
published in	wds:Q69847405-C9A3C12B-77EA-45BE-8E9D-8EBBA0FB483C
published in	Journal of Molecular Biology
issue	wds:Q69847405-282F7BE4-5735-4995-B2DE-E2B4581041F4
volume	wds:Q69847405-8CA8A4EA-3C73-4C55-9F56-76C5C8B62DE7
issue	1
volume	204
DOI	wds:Q69847405-4CCA1500-AC72-4BD3-8AA9-A2BDF954EBCC
DOI	http://dx.doi.org/10.1016/0022-2836(88)90609-2
DOI	10.1016/0022-2836(88)90609-2
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q69847405
is cites work of	Nucleotide sequence of the traI (helicase I) gene from the sex factor F. Engineered proteins detect spontaneous DNA breakage in human and bacterial cells Escherichia coli DNA helicases: mechanisms of DNA unwinding DNA Helicases of Escherichia coli Analysis of the sequence and gene products of the transfer region of the F sex factor Intervening sequences of regularly spaced prokaryotic repeats derive from foreign genetic elements Chemical shift assignments for F-plasmid TraI (381-569). Agrobacterium rhizogenes GALLS protein substitutes for Agrobacterium tumefaciens single-stranded DNA-binding protein VirE2. Genetic analysis of the mobilization and leading regions of the IncN plasmids pKM101 and pCU1 Protein and DNA effectors control the TraI conjugative helicase of plasmid R1. The tra region of the nopaline-type Ti plasmid is a chimera with elements related to the transfer systems of RSF1010, RP4, and F traY and traI are required for oriT-dependent enhanced recombination between lac-containing plasmids and lambda plac5 Structural Insights into Single-Stranded DNA Binding and Cleavage by F Factor TraI Characterization of the Escherichia coli F factor traY gene product and its binding sites Extent of Single-stranded DNA Required for Efficient TraI Helicase Activityin Vitro Revisiting the molecular evolutionary history of Shigella spp. Translocation of DNA across bacterial membranes. Nucleotide sequence and functions of the oriT operon in IncI1 plasmid R64 General mutagenesis of F plasmid TraI reveals its role in conjugative regulation A Novel Fold in the TraI Relaxase–Helicase C-Terminal Domain Is Essential for Conjugative DNA Transfer The F-plasmid TraI protein contains three functional domains required for conjugative DNA strand transfer Single-stranded DNA binding by F TraI relaxase and helicase domains is coordinately regulated Functional characterization of the multidomain F plasmid TraI relaxase-helicase. Characterization of the reaction product of the oriT nicking reaction catalyzed by Escherichia coli DNA helicase I. Plasmid r1 conjugative DNA processing is regulated at the coupling protein interface. Subdomain organization and catalytic residues of the F factor TraI relaxase domain Disrupting antibiotic resistance propagation by inhibiting the conjugative DNA relaxase Escherichia coli DNA helicase I catalyzes a site- and strand-specific nicking reaction at the F plasmid oriT F plasmid conjugative DNA transfer: the TraI helicase activity is essential for DNA strand transfer Characterization of traX, the F plasmid locus required for acetylation of F-pilin subunits Purified Escherichia coli F-factor TraY protein binds oriT. Specific DNA binding of the TraM protein to the oriT region of plasmid R100. Endonuclease activity of Escherichia coli DNA helicase I directed against the transfer origin of the F factor. Gene discovery within the planctomycete division of the domain Bacteria using sequence tags from genomic DNA libraries Conjugation-independent, site-specific recombination at the oriT of the IncW plasmid R388 mediated by TrwC. The Origin of Mutants Under Selection: How Natural Selection Mimics Mutagenesis (Adaptive Mutation) Structure-function analysis of Escherichia coli DNA helicase I reveals non-overlapping transesterase and helicase domains. Frequency of conjugative transfer of plasmid-encoded ISEcp1 - blaCTX-M-15 and aac(6')-lb-cr genes in Enterobacteriaceae at a tertiary care center in Lebanon - role of transferases Specific effects of a recB mutation on the HfrH strain of Escherichia coli.
is cites work of	wds:Q35609800-D86DDC84-E48A-48CA-87FA-4C17C040B8EB wds:Q59264375-F9EA5DD0-1B94-4BF0-8FCA-A219C3A6E1B9 wds:Q62710214-FCB21B52-9571-4B24-8D91-89412DFF36C2 wds:Q35586440-B8E1F330-3344-4220-A3F9-BD00FB5034E6 wds:Q39945437-08FAA071-2ED6-494A-A669-DEA3F3064608 wds:Q39932074-1A1B7B82-DB27-4095-A367-2BF5ABD67972 wds:Q54538025-26608B60-DE5C-4CFB-BF0A-1DFB82D16A80 wds:Q34752571-D64E8937-0A5E-47BA-A0FA-6DE2CC7AF91B wds:Q37178798-3D2C9511-8EA6-46F6-903D-3A2A1B8B5449 wds:Q41082261-07D6FAB1-B800-481F-AB42-6D1214208046 wds:Q42086224-0C9D2176-C61E-458E-811A-83F999ADD88F wds:Q51095151-59B7B6B2-6CF7-4C17-A8EC-9E5EA2A63593 wds:Q27653385-D625E975-028A-47D8-97AE-8D9911E0008C wds:Q24796593-EBA51893-9B15-466C-9120-0E466FE95854 wds:Q33699906-E7192F47-5052-486A-BD2D-6A31B4FAF705 wds:Q36257927-D57D62D7-9D00-4E4C-9C74-C252D3AC592D wds:Q35225286-906F1BFD-DF7A-4844-BD65-15846BF28EC3 wds:Q35028595-A4BDB0C1-F4DD-4E65-85AB-304AA4C366FE wds:Q40816202-DDAB1913-E224-4632-9C7C-6276142E3160 wds:Q42612963-5D0FDB0B-3197-4110-B308-BDDEEA548504 wds:Q24674141-29DBC5A7-DF95-44EE-86AF-0F1DCFE3D762 wds:Q33963016-DBA51F18-DC02-42BF-AEAB-71474E6FBBE2 wds:Q41813525-E80F7E7C-5588-4319-8BC3-DEC307A722AE wds:Q40693778-AA66649F-5645-4B2D-AD61-309F4D94874D

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