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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
1997-10-15
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pubmed:abstractText |
13S condensin is a five-subunit protein complex that plays a central role in mitotic chromosome condensation in Xenopus egg extracts. Two core subunits of this complex, XCAP-C and XCAP-E, belong to an emerging family of putative ATPases, the SMC family. We report here that 13S condensin has a DNA-stimulated ATPase activity and exhibits a high affinity for structured DNAs such as cruciform DNA. 13S condensin is able to introduce positive supercoils into a closed circular DNA in the presence of bacterial or eukaryotic topoisomerase I. The supercoiling reaction is ATP-dependent. We propose that 13S condensin wraps DNA in a right-handed direction by utilizing the energy of ATP hydrolysis. This reaction may represent a key mechanism underlying the compaction of chromatin fibers during mitosis.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Chromatin,
http://linkedlifedata.com/resource/pubmed/chemical/Chromosomal Proteins, Non-Histone,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Circular,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Superhelical,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Topoisomerases, Type I,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Multiprotein Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/NCAPH protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SMC2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/XCAP-C protein, Xenopus,
http://linkedlifedata.com/resource/pubmed/chemical/XCAP-E protein, Xenopus,
http://linkedlifedata.com/resource/pubmed/chemical/Xenopus Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/condensin complexes
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
22
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pubmed:volume |
90
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
625-34
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9288743-Adenosine Triphosphatases,
pubmed-meshheading:9288743-Adenosine Triphosphate,
pubmed-meshheading:9288743-Animals,
pubmed-meshheading:9288743-Carrier Proteins,
pubmed-meshheading:9288743-Cell Cycle Proteins,
pubmed-meshheading:9288743-Chromatin,
pubmed-meshheading:9288743-Chromosomal Proteins, Non-Histone,
pubmed-meshheading:9288743-Chromosomes,
pubmed-meshheading:9288743-DNA, Circular,
pubmed-meshheading:9288743-DNA, Superhelical,
pubmed-meshheading:9288743-DNA Helicases,
pubmed-meshheading:9288743-DNA Topoisomerases, Type I,
pubmed-meshheading:9288743-DNA-Binding Proteins,
pubmed-meshheading:9288743-Hydrolysis,
pubmed-meshheading:9288743-Multiprotein Complexes,
pubmed-meshheading:9288743-Nuclear Proteins,
pubmed-meshheading:9288743-Nucleic Acid Conformation,
pubmed-meshheading:9288743-Oocytes,
pubmed-meshheading:9288743-Xenopus,
pubmed-meshheading:9288743-Xenopus Proteins
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pubmed:year |
1997
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pubmed:articleTitle |
ATP-dependent positive supercoiling of DNA by 13S condensin: a biochemical implication for chromosome condensation.
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pubmed:affiliation |
Cold Spring Harbor Laboratory, New York 11724, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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