Source:http://linkedlifedata.com/resource/pubmed/id/19696745
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
19
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pubmed:dateCreated |
2009-10-7
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pubmed:abstractText |
Mutations in RECQ4, a member of the RecQ family of DNA helicases, have been linked to the progeroid disease Rothmund-Thomson Syndrome. Attempts to understand the complex phenotypes observed in recq4-deficient cells suggest a potential involvement in DNA repair and replication, yet the molecular basis of the function of RECQ4 in these processes remains unknown. Here, we report the identification of a highly purified chromatin-bound RECQ4 complex from human cell extracts. We found that essential replisome factors MCM10, MCM2-7 helicase, CDC45 and GINS are the primary interaction partner proteins of human RECQ4. Importantly, complex formation and the association of RECQ4 with the replication origin are cell-cycle regulated. Furthermore, we show that MCM10 is essential for the integrity of the RECQ4-MCM replicative helicase complex. MCM10 interacts directly with RECQ4 and regulates its DNA unwinding activity, and that this interaction may be modulated by cyclin-dependent kinase phosphorylation. Thus, these studies show that RECQ4 is an integral component of the MCM replicative helicase complex participating in DNA replication in human cells.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Chromatin,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/MCM10 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/MCM2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/MCM7 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RECQL4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/RecQ Helicases
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1460-2075
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
7
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pubmed:volume |
28
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3005-14
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pubmed:dateRevised |
2010-10-8
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pubmed:meshHeading |
pubmed-meshheading:19696745-Animals,
pubmed-meshheading:19696745-Cell Cycle,
pubmed-meshheading:19696745-Cell Cycle Proteins,
pubmed-meshheading:19696745-Cell Line,
pubmed-meshheading:19696745-Chromatin,
pubmed-meshheading:19696745-DNA,
pubmed-meshheading:19696745-DNA Replication,
pubmed-meshheading:19696745-DNA-Binding Proteins,
pubmed-meshheading:19696745-Humans,
pubmed-meshheading:19696745-Nuclear Proteins,
pubmed-meshheading:19696745-RecQ Helicases,
pubmed-meshheading:19696745-Replication Origin
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pubmed:year |
2009
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pubmed:articleTitle |
MCM10 mediates RECQ4 association with MCM2-7 helicase complex during DNA replication.
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pubmed:affiliation |
Department of Therapeutic Radiology, Yale University School of Medicine, New Haven, CT 06520-8040, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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