Structural highlights
Function
CPSF1_HUMAN Component of the cleavage and polyadenylation specificity factor (CPSF) complex that plays a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. This subunit is involved in the RNA recognition step of the polyadenylation reaction.[1]
Publication Abstract from PubMed
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-A-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.
Structural basis of AAUAAA polyadenylation signal recognition by the human CPSF complex.,Clerici M, Faini M, Muckenfuss LM, Aebersold R, Jinek M Nat Struct Mol Biol. 2018 Jan 22. pii: 10.1038/s41594-017-0020-6. doi:, 10.1038/s41594-017-0020-6. PMID:29358758[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kaufmann I, Martin G, Friedlein A, Langen H, Keller W. Human Fip1 is a subunit of CPSF that binds to U-rich RNA elements and stimulates poly(A) polymerase. EMBO J. 2004 Feb 11;23(3):616-26. Epub 2004 Jan 29. PMID:14749727 doi:http://dx.doi.org/10.1038/sj.emboj.7600070
- ↑ Clerici M, Faini M, Muckenfuss LM, Aebersold R, Jinek M. Structural basis of AAUAAA polyadenylation signal recognition by the human CPSF complex. Nat Struct Mol Biol. 2018 Jan 22. pii: 10.1038/s41594-017-0020-6. doi:, 10.1038/s41594-017-0020-6. PMID:29358758 doi:http://dx.doi.org/10.1038/s41594-017-0020-6
