期刊
SCIENCE
卷 358, 期 6366, 页码 1056-1059出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aao6535
关键词
-
资金
- European Molecular Biology Organization Long-Term Fellowship - European Commission through Marie Curie Actions [ALTF66-2015, LTFCOFUND2013, GA-2013-609409]
- Gates Cambridge
- European Research Council under the European Union [261151]
- European Union [725685]
- ERC [695511]
- Medical Research Council (MRC) [MC_U105192715, MC_U105185859]
- Wellcome Trust [EM15622]
- MRC
- Biotechnology and Biological Sciences Research Council
- European Research Council (ERC) [261151] Funding Source: European Research Council (ERC)
- Medical Research Council [MC_U105192715, MC_UP_A025_1012, MC_U105185859] Funding Source: researchfish
- MRC [MC_U105192715, MC_U105185859, MC_UP_A025_1012] Funding Source: UKRI
Newly transcribed eukaryotic precursor messenger RNAs (pre-mRNAs) are processed at their 3' ends by the similar to 1-megadalton multiprotein cleavage and polyadenylation factor (CPF). CPF cleaves pre-mRNAs, adds a polyadenylate tail, and triggers transcription termination, but it is unclear how its various enzymes are coordinated and assembled. Here, we show that the nuclease, polymerase, and phosphatase activities of yeast CPF are organized into three modules. Using electron cryomicroscopy, we determined a 3.5-angstrom-resolution structure of the similar to 200-kilodalton polymerase module. This revealed four beta propellers, in an assembly markedly similar to those of other protein complexes that bind nucleic acid. Combined with in vitro reconstitution experiments, our data show that the polymerase module brings together factors required for specific and efficient polyadenylation, to help coordinate mRNA 3 '-end processing.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据