6EOJ

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

Summary for 6EOJ

• Entry DOI: 10.2210/pdb6eoj/pdb
• EMDB information: 3908
• Descriptor: Protein CFT1, mRNA 3'-end-processing protein YTH1, Polyadenylation factor subunit 2,Polyadenylation factor subunit 2, ... (4 entities in total)
• Functional Keywords: wd40, beta-propeller, zinc finger, 3'end processing, rna binding protein
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); More
• Cellular location: Nucleus : Q06632 Q06102
• Total number of polymer chains: 3
• Total formula weight: 231905.03

Authors

Casanal, A.,Kumar, A.,Hill, C.H.,Emsley, P.,Passmore, L.A. (deposition date: 2017-10-09, release date: 2017-11-15, Last modification date: 2024-05-15)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (3.55 Å)