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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
1992-11-16
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pubmed:abstractText |
A murine cardiac lambda gt11 expression library was screened with an amphipathic helix antibody, and a recombinant representing the C-terminal 194 residues of murine HSP90 (HSP84) was cloned. Both recombinant and native HSP90s were then found to rapidly convert a basic helix-loop-helix protein (MyoD1) from an inactive to an active conformation, as assayed by sequence-specific DNA binding. The conversion process involves a transient interaction between HSP90 and MyoD1 and does not result in the formation of a stable tertiary complex. Conversion does not require ATP and occurs stoichiometrically in a dose-dependent fashion. HSP90 is an abundant, ubiquitous, and highly conserved protein present in most eukaryotic cells. These results provide direct evidence that HSP90 can affect the conformational structure of a DNA-binding protein.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1406681-1310896,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1406681-1731198,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1406681-1846704,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1406681-1852076,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1406681-1855252,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1406681-2234079,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1406681-2243115,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1406681-2376573,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1406681-2426456,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1406681-2445630,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1406681-2503252,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1406681-2527334,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1406681-2536161,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1406681-2550138,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1406681-2584195,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1406681-2626012,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1406681-2761542,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1406681-2843537,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1406681-3062385,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1406681-3175662,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1406681-3289117,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1406681-3294824,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1406681-3301534,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1406681-3413062,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1406681-3427028,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1406681-3530253,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1406681-354496,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1406681-3550435,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1406681-3782106,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1406681-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1406681-6100915,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1406681-6262754,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1406681-6269742,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1406681-6325446,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1406681-6396506
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0270-7306
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5059-68
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pubmed:dateRevised |
2010-9-7
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pubmed:meshHeading |
pubmed-meshheading:1406681-Allosteric Regulation,
pubmed-meshheading:1406681-Amino Acid Sequence,
pubmed-meshheading:1406681-Animals,
pubmed-meshheading:1406681-Base Sequence,
pubmed-meshheading:1406681-Cloning, Molecular,
pubmed-meshheading:1406681-DNA,
pubmed-meshheading:1406681-Escherichia coli,
pubmed-meshheading:1406681-Heat-Shock Proteins,
pubmed-meshheading:1406681-Mice,
pubmed-meshheading:1406681-Molecular Sequence Data,
pubmed-meshheading:1406681-MyoD Protein,
pubmed-meshheading:1406681-Nuclear Proteins,
pubmed-meshheading:1406681-Phosphoproteins,
pubmed-meshheading:1406681-Protein Binding,
pubmed-meshheading:1406681-Protein Conformation,
pubmed-meshheading:1406681-Protein Denaturation,
pubmed-meshheading:1406681-Sequence Homology, Amino Acid
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pubmed:year |
1992
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pubmed:articleTitle |
Conformational activation of a basic helix-loop-helix protein (MyoD1) by the C-terminal region of murine HSP90 (HSP84).
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pubmed:affiliation |
Department of Pathology, Mount Sinai School of Medicine, New York, New York 10029.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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