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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1992-5-1
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pubmed:abstractText |
The high mobility group (HMG) domain is a DNA-binding motif that is associated with several eukaryotic regulatory proteins, including the lymphoid enhancer-binding factor LEF-1 and the testis-determining factor SRY. Here, we provide evidence that DNA binding by the HMG domain of LEF-1 involves primarily minor groove contacts and induces a bend of approximately 130 degrees in the DNA helix. Bending was also found to accompany sequence-specific DNA binding by the SRY-HMG domain. Examining possible regulatory roles of HMG domain-induced DNA bends, we found that LEF-1 can function in a manner similar to bacterial integration host factor and facilitate communication between widely separated protein-binding sites in a recombination assay. Together with the previous observation that LEF-1 by itself is unable to augment basal promoter activity, these data suggest that HMG domain proteins can serve as "architectural" elements in the assembly of higher-order nucleoprotein structures.
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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/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Nucleotidyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/High Mobility Group Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Integrases,
http://linkedlifedata.com/resource/pubmed/chemical/LEF1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Lymphoid Enhancer-Binding Factor 1,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/SRY protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Sex-Determining Region Y Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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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 |
3
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pubmed:volume |
69
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
185-95
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1555239-Base Sequence,
pubmed-meshheading:1555239-Binding Sites,
pubmed-meshheading:1555239-DNA,
pubmed-meshheading:1555239-DNA Nucleotidyltransferases,
pubmed-meshheading:1555239-DNA-Binding Proteins,
pubmed-meshheading:1555239-High Mobility Group Proteins,
pubmed-meshheading:1555239-Humans,
pubmed-meshheading:1555239-Integrases,
pubmed-meshheading:1555239-Lymphoid Enhancer-Binding Factor 1,
pubmed-meshheading:1555239-Molecular Sequence Data,
pubmed-meshheading:1555239-Nuclear Proteins,
pubmed-meshheading:1555239-Nucleic Acid Conformation,
pubmed-meshheading:1555239-Nucleoproteins,
pubmed-meshheading:1555239-Recombination, Genetic,
pubmed-meshheading:1555239-Sex-Determining Region Y Protein,
pubmed-meshheading:1555239-Transcription Factors
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pubmed:year |
1992
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pubmed:articleTitle |
The HMG domain of lymphoid enhancer factor 1 bends DNA and facilitates assembly of functional nucleoprotein structures.
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pubmed:affiliation |
Howard Hughes Medical Institute, Department of Microbiology, University of California, San Francisco 94143-0414.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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