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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
48
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pubmed:dateCreated |
1999-12-29
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pubmed:databankReference |
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pubmed:abstractText |
Using a yeast two-hybrid system with the 70-kDa heat shock cognate protein (hsc70) or its C-terminal 30-kDa domain as baits, we isolated several proteins interacting with hsc70, including Hip/p48 and p60/Hop. Both are known to interact with hsc70. Except for Hip/p48, all of the proteins that we isolated interact with the 30-kDa domain. Moreover, the EEVD motif at the C terminus of the 30-kDa domain appears essential for this interaction. Sequence analysis of these hsc70-interacting proteins reveals that they all contain tetratricopeptide repeats. Using deletion mutants of these proteins, we demonstrated either by two-hybrid or in vitro binding assays that the tetratricopeptide repeat domains in these proteins are necessary and sufficient for mediating the interaction with hsc70.
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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/Antigens, Neoplasm,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/HSC70 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HSP70 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HSPA8 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Hip chaperone,
http://linkedlifedata.com/resource/pubmed/chemical/Hspa8 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SGTA protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Sgta protein, rat
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
26
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pubmed:volume |
274
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
34425-32
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10567422-Amino Acid Sequence,
pubmed-meshheading:10567422-Animals,
pubmed-meshheading:10567422-Antigens, Neoplasm,
pubmed-meshheading:10567422-Binding Sites,
pubmed-meshheading:10567422-Carrier Proteins,
pubmed-meshheading:10567422-Glutathione Transferase,
pubmed-meshheading:10567422-HSC70 Heat-Shock Proteins,
pubmed-meshheading:10567422-HSP70 Heat-Shock Proteins,
pubmed-meshheading:10567422-Humans,
pubmed-meshheading:10567422-Molecular Chaperones,
pubmed-meshheading:10567422-Molecular Sequence Data,
pubmed-meshheading:10567422-Mutation,
pubmed-meshheading:10567422-Protein Binding,
pubmed-meshheading:10567422-Protein Structure, Tertiary,
pubmed-meshheading:10567422-Proteins,
pubmed-meshheading:10567422-Rats,
pubmed-meshheading:10567422-Recombinant Fusion Proteins,
pubmed-meshheading:10567422-Repetitive Sequences, Amino Acid,
pubmed-meshheading:10567422-Two-Hybrid System Techniques
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pubmed:year |
1999
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pubmed:articleTitle |
Specific interaction of the 70-kDa heat shock cognate protein with the tetratricopeptide repeats.
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pubmed:affiliation |
Institute of Molecular Biology, Academia Sinica, Taipei, Taiwan, Republic of China.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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