<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Ristic D</submitter><funding>NCI NIH HHS</funding><pagination>155-67</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3017611</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>39(1)</volume><pubmed_abstract>The defining event in homologous recombination is the exchange of base-paired partners between a single-stranded (ss) DNA and a homologous duplex driven by recombinase proteins, such as human RAD51. To understand the mechanism of this essential genome maintenance event, we analyzed the structure of RAD51-DNA complexes representing strand exchange intermediates at nanometer resolution by scanning force microscopy. Joint molecules were formed between substrates with a defined ssDNA segment and homologous region on a double-stranded (ds) partner. We discovered and quantified several notable architectural features of RAD51 joint molecules. Each end of the RAD51-bound joints had a distinct structure. Using linear substrates, a 10-nt region of mispaired bases blocked extension of joint molecules</pubmed_abstract><journal>Nucleic acids research</journal><pubmed_title>Visualizing RAD51-mediated joint molecules: implications for recombination mechanism and the effect of sequence heterology.</pubmed_title><pmcid>PMC3017611</pmcid><funding_grant_id>5P01CA092584</funding_grant_id><funding_grant_id>P01 CA092584</funding_grant_id><pubmed_authors>Kanaar R</pubmed_authors><pubmed_authors>Ristic D</pubmed_authors><pubmed_authors>Wyman C</pubmed_authors></additional><is_claimable>false</is_claimable><name>Visualizing RAD51-mediated joint molecules: implications for recombination mechanism and the effect of sequence heterology.</name><description>The defining event in homologous recombination is the exchange of base-paired partners between a single-stranded (ss) DNA and a homologous duplex driven by recombinase proteins, such as human RAD51. To understand the mechanism of this essential genome maintenance event, we analyzed the structure of RAD51-DNA complexes representing strand exchange intermediates at nanometer resolution by scanning force microscopy. Joint molecules were formed between substrates with a defined ssDNA segment and homologous region on a double-stranded (ds) partner. We discovered and quantified several notable architectural features of RAD51 joint molecules. Each end of the RAD51-bound joints had a distinct structure. Using linear substrates, a 10-nt region of mispaired bases blocked extension of joint molecules</description><dates><release>2011-01-01T00:00:00Z</release><publication>2011 Jan</publication><modification>2025-04-04T19:18:16.357Z</modification><creation>2019-03-27T00:37:57Z</creation></dates><accession>S-EPMC3017611</accession><cross_references><pubmed>20817928</pubmed><doi>10.1093/nar/gkq766</doi></cross_references></HashMap>