6EOJ

PolyA polymerase module of the cleavage and polyadenylation factor (CPF) from Saccharomyces cerevisiae

6EOJ の概要

• エントリーDOI: 10.2210/pdb6eoj/pdb
• EMDBエントリー: 3908
• 分子名称: Protein CFT1, mRNA 3'-end-processing protein YTH1, Polyadenylation factor subunit 2,Polyadenylation factor subunit 2, ... (4 entities in total)
• 機能のキーワード: wd40, beta-propeller, zinc finger, 3'end processing, rna binding protein
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); 詳細
• 細胞内の位置: Nucleus : Q06632 Q06102
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 231905.03

構造登録者

Casanal, A.,Kumar, A.,Hill, C.H.,Emsley, P.,Passmore, L.A. (登録日: 2017-10-09, 公開日: 2017-11-15, 最終更新日: 2024-05-15)

主引用文献

Casanal, A.,Kumar, A.,Hill, C.H.,Easter, A.D.,Emsley, P.,Degliesposti, G.,Gordiyenko, Y.,Santhanam, B.,Wolf, J.,Wiederhold, K.,Dornan, G.L.,Skehel, M.,Robinson, C.V.,Passmore, L.A.
Architecture of eukaryotic mRNA 3'-end processing machinery.
Science, 358:1056-1059, 2017

PubMed Abstract: 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.

PubMed: 29074584
DOI: 10.1126/science.aao6535

実験手法

ELECTRON MICROSCOPY (3.55 Å)