Correlation between physiological and transforming activities of the c-mos proto-oncogene product and identification of an essential Mos domain for these activities.
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-box, is essential for all three activities. These results indicate that the in vitro transforming activity of Mos can be ascribed to the same kinase activity of Mos that exerts the physiological activities.
Okazaki
K
K
Division of Molecular Genetics, Institute of Life Science, Kurume University, Fukuoka.
Furuno
N
N
Watanabe
N
N
Ikawa
Y
Y
Vande Woude
G F
GF
Sagata
N
N
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002455:Cell Division; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D015345:Oligonucleotide Probes; D009865:Oocytes / Q000166:cytology / Q000502:physiology; D011505:Protein-Tyrosine Kinases / Q000502:physiology*; D000090063:Proto-Oncogene Mas; D011518:Proto-Oncogene Proteins / Q000502:physiology*; D017231:Proto-Oncogene Proteins c-mos; D011519:Proto-Oncogenes; D014162:Transfection; D014981:Xenopus
C000715470:MAS1 protein, human; D015345:Oligonucleotide Probes; D000090063:Proto-Oncogene Mas; D011518:Proto-Oncogene Proteins; D011505:Protein-Tyrosine Kinases; D017231:Proto-Oncogene Proteins c-mos