TY - JOUR
T1 - An interaction between p21ras and heat shock protein hsp60, a chaperonin
AU - Ikawa, Shuntaro
AU - Weinberg, Robert A.
PY - 1992
Y1 - 1992
N2 - 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.
AB - 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.
KW - Molecular chaperon
KW - Oncogenes
KW - Signal transduction
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UR - http://www.scopus.com/inward/citedby.url?scp=0026610981&partnerID=8YFLogxK
U2 - 10.1073/pnas.89.6.2012
DO - 10.1073/pnas.89.6.2012
M3 - Article
C2 - 1347942
AN - SCOPUS:0026610981
SN - 0027-8424
VL - 89
SP - 2012
EP - 2016
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 6
ER -