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TitleActivation of the Endonuclease that Defines mRNA 3' Ends Requires Incorporation into an 8-Subunit Core Cleavage and Polyadenylation Factor Complex.
Journal, issue, pagesMol Cell, Vol. 73, Issue 6, Page 1217-1231.e11, Year 2019
Publish dateMar 21, 2019
AuthorsChris H Hill / Vytautė Boreikaitė / Ananthanarayanan Kumar / Ana Casañal / Peter Kubík / Gianluca Degliesposti / Sarah Maslen / Angelica Mariani / Ottilie von Loeffelholz / Mathias Girbig / Mark Skehel / Lori A Passmore /
PubMed AbstractCleavage and polyadenylation factor (CPF/CPSF) is a multi-protein complex essential for formation of eukaryotic mRNA 3' ends. CPF cleaves pre-mRNAs at a specific site and adds a poly(A) tail. The ...Cleavage and polyadenylation factor (CPF/CPSF) is a multi-protein complex essential for formation of eukaryotic mRNA 3' ends. CPF cleaves pre-mRNAs at a specific site and adds a poly(A) tail. The cleavage reaction defines the 3' end of the mature mRNA, and thus the activity of the endonuclease is highly regulated. Here, we show that reconstitution of specific pre-mRNA cleavage with recombinant yeast proteins requires incorporation of the Ysh1 endonuclease into an eight-subunit "CPF" complex. Cleavage also requires the accessory cleavage factors IA and IB, which bind substrate pre-mRNAs and CPF, likely facilitating assembly of an active complex. Using X-ray crystallography, electron microscopy, and mass spectrometry, we determine the structure of Ysh1 bound to Mpe1 and the arrangement of subunits within CPF. Together, our data suggest that the active mRNA 3' end processing machinery is a dynamic assembly that is licensed to cleave only when all protein factors come together at the polyadenylation site.
External linksMol Cell / PubMed:30737185 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.28 - 25.0 Å
Structure data

EMDB-0324:
Negative-stain map of CPFcore
Method: EM (single particle) / Resolution: 25.0 Å

EMDB-0325:
Cryo-EM map of the Ysh1-Mpe1 nuclease complex
Method: EM (single particle) / Resolution: 6.0 Å

PDB-6i1d:
Structure of the Ysh1-Mpe1 nuclease complex from S.cerevisiae
Method: X-RAY DIFFRACTION / Resolution: 2.28 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-GOL:
GLYCEROL / Glycerol

ChemComp-HOH:
WATER / Water

Source
  • Saccharomyces cerevisiae (brewer's yeast)
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
KeywordsGENE REGULATION / pre-mRNA / mRNA / nuclease / endonuclease / cleavage / polyadenylation / polyA / CPF / metallo-beta-lactamase / 3' ends

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