Shuttleworth J, Godfrey R, Colman A
School of Biochemistry, University of Birmingham, UK.
EMBO J. 1990 Oct;9(10):3233-40. doi: 10.1002/j.1460-2075.1990.tb07522.x.
The clone MO15 which codes for a 40 kd protein (p40MO15) with 40% amino acid identity to the human cdc2 protein kinase has been isolated from a Xenopus cDNA library using a synthetic oligonucleotide probe. MO15 mRNA is accumulated during oogenesis, becomes de-adenylated during meiotic maturation, and is degraded after the mid-blastula-transition stage of embryogenesis. Translation of p40MO15 is restricted to non-mature oocytes. Specific inhibition of p40MO15 synthesis in stage VI oocytes by antisense oligonucleotide depletion of MO15 mRNA increases the rate of progesterone induced H1 kinase activation and oocyte maturation. This effect can be reversed by subsequent injection of synthetic MO15 mRNA. These results suggest that p40MO15 is involved in negatively regulating meiosis.
已使用合成寡核苷酸探针从非洲爪蟾cDNA文库中分离出克隆MO15,它编码一种40kd的蛋白质(p40MO15),与人类细胞周期蛋白依赖性激酶2(cdc2蛋白激酶)有40%的氨基酸同源性。MO15 mRNA在卵子发生过程中积累,在减数分裂成熟过程中去腺苷酸化,并在胚胎发育的囊胚中期转换阶段后降解。p40MO15的翻译仅限于未成熟的卵母细胞。通过反义寡核苷酸耗尽MO15 mRNA来特异性抑制VI期卵母细胞中p40MO15的合成,可提高孕酮诱导的H1激酶激活率和卵母细胞成熟率。随后注射合成的MO15 mRNA可逆转这种效应。这些结果表明p40MO15参与减数分裂的负调控。