哺乳动物的GLD-2同源物是聚腺苷酸聚合酶。
Mammalian GLD-2 homologs are poly(A) polymerases.
作者信息
Kwak Jae Eun, Wang Liaoteng, Ballantyne Scott, Kimble Judith, Wickens Marvin
机构信息
Department of Biochemistry, 433 Babcock Drive, University of Wisconsin, Madison, WI 53706-1544, USA.
出版信息
Proc Natl Acad Sci U S A. 2004 Mar 30;101(13):4407-12. doi: 10.1073/pnas.0400779101.
GLD-2 is a cytoplasmic poly(A) polymerase present in the Caenorhabditis elegans germ line and embryo. It is a divergent member of the DNA polymerase beta nucleotidyl transferase superfamily, which includes CCA-adding enzymes, DNA polymerases and eukaryotic nuclear poly(A) polymerases. The polyadenylation activity of GLD-2 is stimulated by physical interaction with an RNA binding protein, GLD-3. To test whether GLD-3 might stimulate GLD-2 by recruiting it to RNA, we tethered C. elegans GLD-2 to mRNAs in Xenopus oocytes by using MS2 coat protein. Tethered GLD-2 adds poly(A) and stimulates translation of the mRNA, demonstrating that recruitment is sufficient to stimulate polyadenylation activity. We use the same tethered assay to identify human and mouse poly(A) polymerases related to GLD-2. This may provide entrees to previously uncharacterized modes of polyadenylation in mammalian cells.
GLD-2是一种存在于秀丽隐杆线虫生殖系和胚胎中的细胞质多聚腺苷酸聚合酶。它是DNA聚合酶β核苷酸转移酶超家族的一个不同成员，该超家族包括添加CCA的酶、DNA聚合酶和真核细胞核多聚腺苷酸聚合酶。GLD-2的多聚腺苷酸化活性通过与一种RNA结合蛋白GLD-3的物理相互作用而受到刺激。为了测试GLD-3是否可能通过将GLD-2招募到RNA上来刺激它，我们利用MS2外壳蛋白将秀丽隐杆线虫的GLD-2与非洲爪蟾卵母细胞中的mRNA拴系在一起。拴系的GLD-2添加多聚腺苷酸并刺激mRNA的翻译，这表明招募足以刺激多聚腺苷酸化活性。我们使用相同的拴系试验来鉴定与GLD-2相关的人类和小鼠多聚腺苷酸聚合酶。这可能为哺乳动物细胞中以前未被表征的多聚腺苷酸化模式提供切入点。
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