ArticleRNA (New York, N.Y.)2012
Crystal structure of the Rna14-Rna15 complex.
Article in RNA (New York, N.Y.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Molecular Insights into mRNA Polyadenylation and Deadenylation.International journal of molecular sciences · 2022Review
- Molecular mechanism for the interaction between human CPSF30 and hFip1.Genes & development · 2020Article
- Recent molecular insights into canonical pre-mRNA 3'-end processing.Transcription · 2020Review
- Structural Insights into the Human Pre-mRNA 3'-End Processing Machinery.Molecular cell · 2020Article
- Increased versatility despite reduced molecular complexity: evolution, structure and function of metazoan splicing factor PRPF39.Nucleic acids research · 2019Article
- Activation of the Endonuclease that Defines mRNA 3' Ends Requires Incorporation into an 8-Subunit Core Cleavage and Polyadenylation Factor Complex.Molecular cell · 2019Article
- Reconstitution of the CstF complex unveils a regulatory role for CstF-50 in recognition of 3'-end processing signals.Nucleic acids research · 2018Article
- Distinct roles of Pcf11 zinc-binding domains in pre-mRNA 3'-end processing.Nucleic acids research · 2017Article
- The C terminus of Pcf11 forms a novel zinc-finger structure that plays an essential role in mRNA 3'-end processing.RNA (New York, N.Y.) · 2017Article
- Structural Basis of the Recruitment of Ubiquitin-specific Protease USP15 by Spliceosome Recycling Factor SART3.The Journal of biological chemistry · 2016Article
- Structural basis for recruiting and shuttling of the spliceosomal deubiquitinase USP4 by SART3.Nucleic acids research · 2016Article
- Delineating the structural blueprint of the pre-mRNA 3'-end processing machinery.Molecular and cellular biology · 2014Review
- Structure and function of pre-mRNA 5'-end capping quality control and 3'-end processing.Biochemistry · 2014Article
- Structural and biochemical analysis of the assembly and function of the yeast pre-mRNA 3' end processing complex CF I.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
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2 authors.
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Abstract
A large protein machinery is required for 3'-end processing of mRNA precursors in eukaryotes. Cleavage factor IA (CF IA), a complex in the 3'-end processing machinery in yeast, contains four subunits, Rna14, Rna15, Clp1, and Pcf11. Rna14 has a HAT (half a TPR) domain at the N terminus and a region at the C terminus that mediates interactions with Rna15. Rna15 contains a RNA recognition module (RRM) at the N terminus, followed by a hinge region. These two proteins are homologs of CstF-77 and CstF-64 in the cleavage stimulation factor (CstF) of the mammalian 3'-end processing machinery. We report the first crystal structure of Rna14 in complex with the hinge region of Rna15, and the structures of the HAT domain of Rna14 alone in two different crystal forms. The complex of the C-terminal region of Rna14 with the hinge region of Rna15 does not have strong interactions with the HAT domain of Rna14, and this complex is likely to function independently of the HAT domain. Like CstF-77, the HAT domain of Rna14 is also a tightly associated dimer with a highly elongated shape. However, there are large variations in the organization of this dimer among the Rna14 structures, and there are also significant structural differences to CstF-77. These observations suggest that the HAT domain and especially its dimer may have some inherent conformational variability.
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