16537486

Source:http://linkedlifedata.com/resource/pubmed/id/16537486

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0033414, umls-concept:C0205103, umls-concept:C0599773, umls-concept:C1835856
pubmed:issue	11
pubmed:dateCreated	2006-3-15
pubmed:abstractText	BLM encodes a member of the highly conserved RecQ DNA helicase family, which is essential for the maintenance of genome stability. Homozygous inactivation of BLM gives rise to the cancer predisposition disorder Bloom's syndrome. A common feature of many RecQ helicase mutants is a hyperrecombination phenotype. In Bloom's syndrome, this phenotype manifests as an elevated frequency of sister chromatid exchanges and interhomologue recombination. We have shown previously that BLM, together with its evolutionarily conserved binding partner topoisomerase IIIalpha (hTOPO IIIalpha), can process recombination intermediates that contain double Holliday junctions into noncrossover products by a mechanism termed dissolution. Here we show that a recently identified third component of the human BLM/hTOPO IIIalpha complex, BLAP75/RMI1, promotes dissolution catalyzed by hTOPO IIIalpha. This activity of BLAP75/RMI1 is specific for dissolution catalyzed by hTOPO IIIalpha because it has no effect in reactions containing either Escherichia coli Top1 or Top3, both of which can also catalyze dissolution in a BLM-dependent manner. We present evidence that BLAP75/RMI1 acts by recruiting hTOPO IIIalpha to double Holliday junctions. Implications of the conserved ability of type IA topoisomerases to catalyze dissolution and how the evolution of factors such as BLAP75/RMI1 might confer specificity on the execution of this process are discussed.
pubmed:grant	http://linkedlifedata.com/resource/pubmed/grant/CA91029, http://linkedlifedata.com/resource/pubmed/grant/CA97175
pubmed:commentsCorrections	http://linkedlifedata.com/resource/pubmed/commentcorrection/16537486-10360177, http://linkedlifedata.com/resource/pubmed/commentcorrection/16537486-10373565, http://linkedlifedata.com/resource/pubmed/commentcorrection/16537486-10497270, http://linkedlifedata.com/resource/pubmed/commentcorrection/16537486-10572171, http://linkedlifedata.com/resource/pubmed/commentcorrection/16537486-10728666, http://linkedlifedata.com/resource/pubmed/commentcorrection/16537486-10734115, http://linkedlifedata.com/resource/pubmed/commentcorrection/16537486-10823897, http://linkedlifedata.com/resource/pubmed/commentcorrection/16537486-11087418, http://linkedlifedata.com/resource/pubmed/commentcorrection/16537486-11433031, http://linkedlifedata.com/resource/pubmed/commentcorrection/16537486-11497238, http://linkedlifedata.com/resource/pubmed/commentcorrection/16537486-12399378, http://linkedlifedata.com/resource/pubmed/commentcorrection/16537486-12415303, http://linkedlifedata.com/resource/pubmed/commentcorrection/16537486-12509234, http://linkedlifedata.com/resource/pubmed/commentcorrection/16537486-12612652, http://linkedlifedata.com/resource/pubmed/commentcorrection/16537486-12724401, http://linkedlifedata.com/resource/pubmed/commentcorrection/16537486-12803543, http://linkedlifedata.com/resource/pubmed/commentcorrection/16537486-1321123, http://linkedlifedata.com/resource/pubmed/commentcorrection/16537486-14622595, http://linkedlifedata.com/resource/pubmed/commentcorrection/16537486-14685245, http://linkedlifedata.com/resource/pubmed/commentcorrection/16537486-14738748, http://linkedlifedata.com/resource/pubmed/commentcorrection/16537486-15775963, http://linkedlifedata.com/resource/pubmed/commentcorrection/16537486-15889139, http://linkedlifedata.com/resource/pubmed/commentcorrection/16537486-15899853, http://linkedlifedata.com/resource/pubmed/commentcorrection/16537486-15990871, http://linkedlifedata.com/resource/pubmed/commentcorrection/16537486-16055725, http://linkedlifedata.com/resource/pubmed/commentcorrection/16537486-2546682, http://linkedlifedata.com/resource/pubmed/commentcorrection/16537486-4140506, http://linkedlifedata.com/resource/pubmed/commentcorrection/16537486-7585968, http://linkedlifedata.com/resource/pubmed/commentcorrection/16537486-7969174, http://linkedlifedata.com/resource/pubmed/commentcorrection/16537486-8107128, http://linkedlifedata.com/resource/pubmed/commentcorrection/16537486-8913739, http://linkedlifedata.com/resource/pubmed/commentcorrection/16537486-9184215, http://linkedlifedata.com/resource/pubmed/commentcorrection/16537486-9388193, http://linkedlifedata.com/resource/pubmed/commentcorrection/16537486-9765292
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/7505876
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Bloom syndrome protein, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DNA, Cruciform, http://linkedlifedata.com/resource/pubmed/chemical/DNA Helicases, http://linkedlifedata.com/resource/pubmed/chemical/DNA Topoisomerases, Type I, http://linkedlifedata.com/resource/pubmed/chemical/Multiprotein Complexes, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RMI1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/RecQ Helicases, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/topoisomerase IIIalpha
pubmed:status	MEDLINE
pubmed:month	Mar
pubmed:issn	0027-8424
pubmed:author	pubmed-author:BachratiCsanad ZCZ, pubmed-author:BrownGrant WGW, pubmed-author:ChangMichaelM, pubmed-author:HicksonIan DID, pubmed-author:LiLeiL, pubmed-author:OuJiongwenJ, pubmed-author:WangWeidongW, pubmed-author:WuLeonardL, pubmed-author:XuChangC, pubmed-author:YinJinhuJ
pubmed:issnType	Print
pubmed:day	14
pubmed:volume	103
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	4068-73
pubmed:dateRevised	2009-11-19
pubmed:meshHeading	pubmed-meshheading:16537486-Adenosine Triphosphatases, pubmed-meshheading:16537486-Bloom Syndrome, pubmed-meshheading:16537486-Carrier Proteins, pubmed-meshheading:16537486-DNA, Cruciform, pubmed-meshheading:16537486-DNA Helicases, pubmed-meshheading:16537486-DNA Topoisomerases, Type I, pubmed-meshheading:16537486-Escherichia coli, pubmed-meshheading:16537486-Humans, pubmed-meshheading:16537486-Multiprotein Complexes, pubmed-meshheading:16537486-Nuclear Proteins, pubmed-meshheading:16537486-Phenotype, pubmed-meshheading:16537486-Protein Binding, pubmed-meshheading:16537486-RecQ Helicases, pubmed-meshheading:16537486-Recombinant Proteins, pubmed-meshheading:16537486-Recombination, Genetic, pubmed-meshheading:16537486-Sister Chromatid Exchange
pubmed:year	2006
pubmed:articleTitle	BLAP75/RMI1 promotes the BLM-dependent dissolution of homologous recombination intermediates.
pubmed:affiliation	Cancer Research UK, Weatherall Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital, Oxford OX3 9DS, United Kingdom.
pubmed:publicationType	Journal Article, In Vitro

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