Open AccessCorrelation between Physiological and Transforming Activities of the c–mos Proto–oncogene Product and Identification of an Essential Mos Domain for These Activities
Author(s) -
Okazaki Kenji,
Furuno Nobuaki,
Watanabe Nobumoto,
Ikawa Yoji,
Vande Woude George F.,
Sagata Noriyuki
Publication year - 1991
Publication title -
japanese journal of cancer research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.035
H-Index - 141
eISSN - 1349-7006
pISSN - 0910-5050
DOI - 10.1111/j.1349-7006.1991.tb01837.x
Subject(s) - xenopus , mutant , in vitro , gene , kinase , biology , microbiology and biotechnology , gene product , phosphorylation , cleavage (geology) , protein kinase domain , amino acid , protein kinase a , chemistry , biochemistry , gene expression , paleontology , fracture (geology)
Using Xenopus eggs and NIH3T3 cells as assay systems, we have compared the physiological (i.e. maturation–inducing and cleavage–arresting) and in vitro transforming activities of the c– mos genes from various species as well as their mutant genes. These analyses show that the three biological activities all depend upon the intrinsic protein kinase activity of Mos and correlate well with each other. Furthermore, our results demonstrate that a well conserved N–terminal 14–amino acid sequence of Mos, termed the Mos–hox, is essential for all three activities. These results indicate that the in vitro transforming activity of Mos can he ascribed to the same kinase activity of Mos that exerts the physiological activities.