Structural highlights
Function
[CSTF1_HUMAN] One of the multiple factors required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. May be responsible for the interaction of CSTF with other factors to form a stable complex on the pre-mRNA. [CSTF3_HUMAN] One of the multiple factors required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs.
Publication Abstract from PubMed
Cleavage stimulation factor (CstF) is a highly conserved protein complex composed of three subunits that recognizes G/U-rich sequences downstream of the polyadenylation signal of eukaryotic mRNAs. While CstF has been identified over 25 years ago, the architecture and contribution of each subunit to RNA recognition have not been fully understood. In this study, we provide a structural basis for the recruitment of CstF-50 to CstF via interaction with CstF-77 and establish that the hexameric assembly of CstF creates a high affinity platform to target various G/U-rich sequences. We further demonstrate that CstF-77 boosts the affinity of the CstF-64 RRM to the RNA targets and CstF-50 fine tunes the ability of the complex to recognize G/U sequences of certain lengths and content.
Reconstitution of the CstF complex unveils a regulatory role for CstF-50 in recognition of 3'-end processing signals.,Yang W, Hsu PL, Yang F, Song JE, Varani G Nucleic Acids Res. 2017 Nov 24. pii: 4647674. doi: 10.1093/nar/gkx1177. PMID:29186539[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yang W, Hsu PL, Yang F, Song JE, Varani G. Reconstitution of the CstF complex unveils a regulatory role for CstF-50 in recognition of 3'-end processing signals. Nucleic Acids Res. 2017 Nov 24. pii: 4647674. doi: 10.1093/nar/gkx1177. PMID:29186539 doi:http://dx.doi.org/10.1093/nar/gkx1177
