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-Structure paper
タイトル | Architecture of eukaryotic mRNA 3'-end processing machinery. |
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ジャーナル・号・ページ | Science, Vol. 358, Issue 6366, Page 1056-1059, Year 2017 |
掲載日 | 2017年11月24日 |
著者 | Ana Casañal / Ananthanarayanan Kumar / Chris H Hill / Ashley D Easter / Paul Emsley / Gianluca Degliesposti / Yuliya Gordiyenko / Balaji Santhanam / Jana Wolf / Katrin Wiederhold / Gillian L Dornan / Mark Skehel / Carol V Robinson / Lori A Passmore / |
PubMed 要旨 | Newly transcribed eukaryotic precursor messenger RNAs (pre-mRNAs) are processed at their 3' ends by the ~1-megadalton multiprotein cleavage and polyadenylation factor (CPF). CPF cleaves pre-mRNAs, ...Newly transcribed eukaryotic precursor messenger RNAs (pre-mRNAs) are processed at their 3' ends by the ~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 ~200-kilodalton polymerase module. This revealed four β 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. |
リンク | Science / PubMed:29074584 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.55 Å |
構造データ | |
化合物 | ChemComp-ZN: |
由来 |
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キーワード | RNA BINDING PROTEIN / WD40 / Beta-propeller / Zinc finger / 3'end processing |