Abstract
Ras proteins play a crucial role in the development of neoplasia and in signal transduction in normal cells. In a search for proteins interacting with p21ras, we previously identified a protein of 60 kDa (p60) through use of a chemical cross-linker. Using information from partial amino acid sequencing of the purified protein, we isolated full-length cDNA clones encoding this 60-kDa protein. Nucleotide sequence analysis revealed that p60 is the murine heat shock protein hsp60, a chaperonin. Association of hsp60 with p21ras appears physiological, as the amount of hsp60 complexed to p21ras was similar even in cells over-expressing p21ras, and reversing the order of cross-linking and lysis of the cells, which releases large amounts of hsp60 from mitochondria, did not alter the amount of hsp60 cross-linked to p21ras.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Antibodies, Monoclonal
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Base Sequence
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Cell Line
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Chaperonins
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Cloning, Molecular
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Cross-Linking Reagents
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Heat-Shock Proteins / genetics
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Heat-Shock Proteins / isolation & purification
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Heat-Shock Proteins / metabolism*
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Humans
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Molecular Sequence Data
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Oligodeoxyribonucleotides / chemical synthesis
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Proteins / genetics
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Proteins / metabolism*
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Proto-Oncogene Proteins p21(ras) / genetics
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Proto-Oncogene Proteins p21(ras) / metabolism*
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Rats
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Sequence Homology, Nucleic Acid
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Succinimides
Substances
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Antibodies, Monoclonal
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Cross-Linking Reagents
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Heat-Shock Proteins
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Oligodeoxyribonucleotides
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Proteins
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Succinimides
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Chaperonins
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HRAS protein, human
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Proto-Oncogene Proteins p21(ras)
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dithiobis(succinimidylpropionate)