Structural basis of AAUAAA polyadenylation signal recognition by the human CPSF complex.
- Clerici M Department of Biochemistry, University of Zurich, Zurich, Switzerland.
- Faini M Department of Biology, Institute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland.
- Muckenfuss LM Department of Biochemistry, University of Zurich, Zurich, Switzerland.
- Aebersold R Department of Biology, Institute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland.
- Jinek M Department of Biochemistry, University of Zurich, Zurich, Switzerland. jinek@bioc.uzh.ch.
- 2018-01-24
Published in:
- Nature structural & molecular biology. - 2018
Amino Acid Motifs
Cleavage And Polyadenylation Specificity Factor
Cryoelectron Microscopy
Humans
Image Processing, Computer-Assisted
Molecular Structure
Motion
Nuclear Proteins
Poly A
Polyadenylation
Protein Binding
Protein Domains
Protein Multimerization
RNA Precursors
RNA, Messenger
English
Mammalian mRNA biogenesis requires specific recognition of a hexanucleotide AAUAAA motif in the polyadenylation signals (PAS) of precursor mRNA (pre-mRNA) transcripts by the cleavage and polyadenylation specificity factor (CPSF) complex. Here we present a 3.1-Å-resolution cryo-EM structure of a core CPSF module bound to the PAS hexamer motif. The structure reveals the molecular interactions responsible for base-specific recognition, providing a rationale for mechanistic differences between mammalian and yeast 3' polyadenylation.
- Language
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- English
- Open access status
- green
- Identifiers
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- DOI 10.1038/s41594-017-0020-6
- PMID 29358758
- Persistent URL
- https://folia.unifr.ch/global/documents/262942
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