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rdf:type |
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lifeskim:mentions |
umls-concept:C0024660,
umls-concept:C0205147,
umls-concept:C0243044,
umls-concept:C0376525,
umls-concept:C0542341,
umls-concept:C1514873,
umls-concept:C1515655,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636,
umls-concept:C1825534
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pubmed:issue |
2
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pubmed:dateCreated |
1994-2-24
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pubmed:abstractText |
The majority of mouse HSP90 exists as alpha-alpha and beta-beta homodimers. Truncation of the 15-kDa carboxy-terminal region of mouse HSP90 by digestion with the Ca(2+)-dependent protease m-calpain caused dissociation of the dimer. When expressed in a reticulocyte lysate, the full-length human HSP90 alpha formed a dimeric form. A plasmid harboring human HSP90 alpha cDNA was constructed so that the carboxy-terminal 49 amino acid residues were removed when translated in vitro. This carboxy-terminally truncated human HSP90 alpha was found to exist as a monomer. In contrast, loss of the 118 amino acid residues from the amino terminus of human HSP90 alpha did not affect its in vitro dimerization. Introduction of an expression plasmid harboring the full-length human HSP90 alpha complements the lethality caused by the double mutations of two HSP90-related genes, hsp82 and hsc82, in a haploid strain of Saccharomyces cerevisiae. The carboxy-terminally truncated human HSP90 alpha neither formed dimers in yeast cells nor rescued the lethal double mutant.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-1376003,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-1406681,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-1537818,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-1551911,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-1629193,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-1731198,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-1939158,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-2005788,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-2016286,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-2037568,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-2184891,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-2199781,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-2234079,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-2266108,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-2405907,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-2414293,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-2445630,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-2507541,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-2556106,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-2584195,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-2674684,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-2780322,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-2853609,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-2925609,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-3197833,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-3301534,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-3360801,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-3427028,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-3534880,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-3611052,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-3768347,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-3782106,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-6088474,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-6262754,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-6269742,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-7174676,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-8423808,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8289821-8486648
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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 |
Feb
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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 |
14
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1459-64
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:8289821-Amino Acid Sequence,
pubmed-meshheading:8289821-Animals,
pubmed-meshheading:8289821-Calpain,
pubmed-meshheading:8289821-Heat-Shock Proteins,
pubmed-meshheading:8289821-Humans,
pubmed-meshheading:8289821-Leukemia L5178,
pubmed-meshheading:8289821-Macromolecular Substances,
pubmed-meshheading:8289821-Mammals,
pubmed-meshheading:8289821-Mice,
pubmed-meshheading:8289821-Molecular Sequence Data,
pubmed-meshheading:8289821-Muscles,
pubmed-meshheading:8289821-Peptide Fragments,
pubmed-meshheading:8289821-Protein Biosynthesis,
pubmed-meshheading:8289821-Rabbits,
pubmed-meshheading:8289821-Restriction Mapping,
pubmed-meshheading:8289821-Saccharomyces cerevisiae,
pubmed-meshheading:8289821-Transcription, Genetic,
pubmed-meshheading:8289821-Tumor Cells, Cultured
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pubmed:year |
1994
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pubmed:articleTitle |
The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo.
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pubmed:affiliation |
Department of Cell Biology, Tokyo Metropolitan Institute of Medical Science, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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