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Article: RecA protein-promoted homologous pairing and strand exchange between intact and partially single-stranded duplex DNA

TitleRecA protein-promoted homologous pairing and strand exchange between intact and partially single-stranded duplex DNA
Authors
Issue Date1992
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/jmb
Citation
Journal Of Molecular Biology, 1992, v. 223 n. 1, p. 79-93 How to Cite?
AbstractIn the pairing reaction between circular gapped and fully duplex DNA, RecA protein first polymerizes on the gapped DNA to form a nucleoprotein filament. Conditions that, removed the formation of secondary structure in the gapped DNA, such as addition of Escherichia coli single-stranded DNA binding protein or preincubation in 1 mM-MgCl2, optimized the binding of RecA protein and increased the formation of joint molecules, The gapped duplex formed stable joints with fully duplex DNA that had a 5' or 3' terminus complementary to the single-stranded region of the gapped molecule. However, the joints formed had distinct properties and structures depending on whether the complementary terminus was at the 5' or 3' end. Pairing between gapped DNA and fully duplex linear DNA with a 3' complementary terminus resulted in strand displacement, symmetric strand exchange and formation of complete strand exchange products. By contrast, pairing between gapped and fully duplex DNA with a 5' complementary terminus produced a joint that was restricted to the gapped region; there was no strand displacement or symmetric strand exchange. The joint formed in the latter reaction was likely a three-stranded intermediate rather than a heteroduplex with the classical Watson-Crick structure. We conclude that, as in the three-strand reaction, the process of strand exchange in the four-strand reaction is polar and progresses in a 5' to 3' direction with respect to the initiating strand. The present study provides further evidence that in both three-strand and four-strand systems the pairing and strand exchange reactions share a common mechanism.
Persistent Identifierhttp://hdl.handle.net/10722/147369
ISSN
2015 Impact Factor: 4.517
2015 SCImago Journal Rankings: 3.002
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorChow, SAen_US
dc.contributor.authorChiu, SKen_US
dc.contributor.authorWong, BCen_US
dc.date.accessioned2012-05-29T06:03:13Z-
dc.date.available2012-05-29T06:03:13Z-
dc.date.issued1992en_US
dc.identifier.citationJournal Of Molecular Biology, 1992, v. 223 n. 1, p. 79-93en_US
dc.identifier.issn0022-2836en_US
dc.identifier.urihttp://hdl.handle.net/10722/147369-
dc.description.abstractIn the pairing reaction between circular gapped and fully duplex DNA, RecA protein first polymerizes on the gapped DNA to form a nucleoprotein filament. Conditions that, removed the formation of secondary structure in the gapped DNA, such as addition of Escherichia coli single-stranded DNA binding protein or preincubation in 1 mM-MgCl2, optimized the binding of RecA protein and increased the formation of joint molecules, The gapped duplex formed stable joints with fully duplex DNA that had a 5' or 3' terminus complementary to the single-stranded region of the gapped molecule. However, the joints formed had distinct properties and structures depending on whether the complementary terminus was at the 5' or 3' end. Pairing between gapped DNA and fully duplex linear DNA with a 3' complementary terminus resulted in strand displacement, symmetric strand exchange and formation of complete strand exchange products. By contrast, pairing between gapped and fully duplex DNA with a 5' complementary terminus produced a joint that was restricted to the gapped region; there was no strand displacement or symmetric strand exchange. The joint formed in the latter reaction was likely a three-stranded intermediate rather than a heteroduplex with the classical Watson-Crick structure. We conclude that, as in the three-strand reaction, the process of strand exchange in the four-strand reaction is polar and progresses in a 5' to 3' direction with respect to the initiating strand. The present study provides further evidence that in both three-strand and four-strand systems the pairing and strand exchange reactions share a common mechanism.en_US
dc.languageengen_US
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/jmben_US
dc.relation.ispartofJournal of Molecular Biologyen_US
dc.subject.meshAdenosine Triphosphatases - Metabolismen_US
dc.subject.meshBacterial Proteins - Metabolismen_US
dc.subject.meshDna, Single-Stranded - Chemistryen_US
dc.subject.meshDna-Binding Proteins - Metabolismen_US
dc.subject.meshEscherichia Colien_US
dc.subject.meshMagnesium - Metabolismen_US
dc.subject.meshNucleic Acid Conformationen_US
dc.subject.meshRec A Recombinases - Metabolismen_US
dc.subject.meshRecombination, Geneticen_US
dc.subject.meshStructure-Activity Relationshipen_US
dc.titleRecA protein-promoted homologous pairing and strand exchange between intact and partially single-stranded duplex DNAen_US
dc.typeArticleen_US
dc.identifier.emailWong, BC:bcwwong@hkucc.hku.hken_US
dc.identifier.authorityWong, BC=rp00369en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/0022-2836(92)90717-Xen_US
dc.identifier.pmid1530979-
dc.identifier.scopuseid_2-s2.0-0026595682en_US
dc.identifier.volume223en_US
dc.identifier.issue1en_US
dc.identifier.spage79en_US
dc.identifier.epage93en_US
dc.identifier.isiWOS:A1992GZ96400010-
dc.publisher.placeUnited Kingdomen_US
dc.identifier.scopusauthoridChow, SA=7201827867en_US
dc.identifier.scopusauthoridChiu, SK=7202291671en_US
dc.identifier.scopusauthoridWong, BC=35733052400en_US

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