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Xenopus homolog of the mos protooncogene transforms mammalian fibroblasts and induces maturation of Xenopus oocytes.


ABSTRACT: The oncogene v-mos transforms mammalian fibroblasts and encodes a serine/threonine protein kinase. Expression of the c-mos protooncogene is most abundant in germ cells, suggesting a normal role for c-mos in meiosis. Here we describe the isolation of cDNA clones containing the complete coding region of the Xenopus laevis homolog of c-mos (mosxe). The mosxe gene is transforming when introduced into murine NIH 3T3 cells, and transformation is abrogated by a lysine-to-arginine mutation in the canonical ATP-binding site. Microinjection of in vitro transcribed mosxe RNA into prophase-arrested Xenopus oocytes causes a resumption of meiosis, leading to germinal vesicle breakdown and oocyte maturation. Oocyte maturation was not observed after microinjection of in vitro transcribed mosxe RNA encoding the lysine-to-arginine mutation. These results demonstrate that the mosxe-encoded protein can induce progression through the cell cycle for both meiotic and mitotic cells and that this property is dependent on the presumptive ATP-binding domain in the protein kinase.

SUBMITTER: Freeman RS 

PROVIDER: S-EPMC297719 | biostudies-other | 1989 Aug

REPOSITORIES: biostudies-other

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Xenopus homolog of the mos protooncogene transforms mammalian fibroblasts and induces maturation of Xenopus oocytes.

Freeman R S RS   Pickham K M KM   Kanki J P JP   Lee B A BA   Pena S V SV   Donoghue D J DJ  

Proceedings of the National Academy of Sciences of the United States of America 19890801 15


The oncogene v-mos transforms mammalian fibroblasts and encodes a serine/threonine protein kinase. Expression of the c-mos protooncogene is most abundant in germ cells, suggesting a normal role for c-mos in meiosis. Here we describe the isolation of cDNA clones containing the complete coding region of the Xenopus laevis homolog of c-mos (mosxe). The mosxe gene is transforming when introduced into murine NIH 3T3 cells, and transformation is abrogated by a lysine-to-arginine mutation in the canoni  ...[more]

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