Mouse cytoplasmic polyadenylylation element binding protein: An evolutionarily conserved protein that interacts with the cytoplasmic polyadenylylation elements of c-mos mRNA

Mouse cytoplasmic polyadenylylation element binding protein: An evolutionarily conserved protein that interacts with the cytoplasmic polyadenylylation elements of c-mos mRNA
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DOI:
10.1073/pnas.93.25.14602
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发表时间:
1996-12-10
影响因子:
11.1
通讯作者:
Richter, JD
Richter, JD
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Gebauer, F;Richter, JD

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细胞质多聚腺苷酸化是在早期发育期间控制母体mRNA翻译的重要过程,并且依赖于3'非翻译区中的两个顺式元件:多聚腺苷酸化六核苷酸AAUAAA和富含U的细胞质多聚腺苷酸化元件(CPE)。在寻找可以介导小鼠c-mos mRNA(编码卵母细胞成熟所必需的丝氨酸/苏氨酸激酶)细胞质聚腺苷酸化的因子时,我们分离出了CPEB的小鼠同源物,CPEB是一种与非洲爪蟾卵母细胞中许多mRNA的CPE结合的蛋白质,是其聚腺苷酸化所必需的。小鼠CPEB(mCPEB)是一种62 kDa的蛋白质,与c-mos mRNA的CPE结合。mCPEB mRNA存在于卵巢、睾丸和肾脏中;在卵巢内,该RNA仅限于卵母细胞。mCPEB与其非洲爪蟾对应物显示80%的总体同一性,在羧基末端部分具有更高的同源性,其包含两个RNA识别基序和半胱氨酸/组氨酸重复。来自节肢动物和线虫的蛋白质也与该区域相似,这表明一种古老且广泛使用的控制多聚腺苷酸化和翻译的机制。
Cytoplasmic polyadenylylation is an essential process that controls the translation of maternal mRNAs during early development and depends on two cis elements in the 3' untranslated region: the polyadenylylation hexanucleotide AAUAAA and a U-rich cytoplasmic polyadenylylation element (CPE). In searching for factors that could mediate cytoplasmic polyadenylylation of mouse c-mos mRNA, which encodes a serine/threonine kinase necessary for oocyte maturation, we have isolated the mouse homolog of CPEB, a protein that binds to the CPEs of a number of mRNAs in Xenopus oocytes and is required for their polyadenylylation. Mouse CPEB (mCPEB) is a 62-kDa protein that binds to the CPEs of c-mos mRNA. mCPEB mRNA is present in the ovary, testis, and kidney; within the ovary, this RNA is restricted to oocytes. mCPEB shows 80% overall identity with its Xenopus counterpart, with a higher homology in the carboxyl-terminal portion, which contains two RNA recognition motifs and a cysteine/histidine repeat. Proteins from arthropods and nematodes are also similar to this region, suggesting an ancient and widely used mechanism to control polyadenylylation and translation.