ArticleNucleic acids research2007
Structure of a nucleotide-bound Clp1-Pcf11 polyadenylation factor.
Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed, 73 citations in OpenAlex.
- hnRNPUL1 has a dead polynucleotide kinase domain that regulates RNA and protein interactions.iScience · 2026Article
- Article
- Systematic Analysis of Diverse Polynucleotide Kinase Clp1 Family Proteins in Eukaryotes: Three Unique Clp1 Proteins of Trypanosoma brucei.Journal of molecular evolution · 2023Article
- CPSF3 Promotes Pre-mRNA Splicing and Prevents CircRNA Cyclization in Hepatocellular Carcinoma.Cancers · 2023Article
- Structural basis of substrate recognition by human tRNA splicing endonuclease TSEN.Nature structural & molecular biology · 2023Article
- Reconstitution of 3' end processing of mammalian pre-mRNA reveals a central role of RBBP6.Genes & development · 2022Article
- PCF11, a Novel CD44-Downstream Transcriptional Target, Linking Its 3'-End Polyadenylation Function to Tumor Cell Metastasis.Frontiers in oncology · 2022Review
- RNA kinase CLP1/Cbc regulates meiosis initiation in spermatogenesis.Human molecular genetics · 2021Article
- CPSF4 regulates circRNA formation and microRNA mediated gene silencing in hepatocellular carcinoma.Oncogene · 2021Article
- Reconstitution of the human tRNA splicing endonuclease complex: insight into the regulation of pre-tRNA cleavage.Nucleic acids research · 2020Article
- Requirement for cleavage factor IIRNA (New York, N.Y.) · 2020Article
- Large-Scale Molecular Evolutionary Analysis Uncovers a Variety of Polynucleotide Kinase Clp1 Family Proteins in the Three Domains of Life.Genome biology and evolution · 2019Article
- Nol9 Is a Spatial Regulator for the Human ITS2 Pre-rRNA Endonuclease-Kinase Complex.Journal of molecular biology · 2019Article
- Cryo-EM reveals active site coordination within a multienzyme pre-rRNA processing complex.Nature structural & molecular biology · 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 mammalian cleavage factor II involved in 3' processing of mRNA precursors.RNA (New York, N.Y.) · 2018Article
- Characterization of the molecular crosstalk within the essential Grc3/Las1 pre-rRNA processing complex.RNA (New York, N.Y.) · 2018Article
- Distinct roles of Pcf11 zinc-binding domains in pre-mRNA 3'-end processing.Nucleic acids research · 2017Article
- Grc3 programs the essential endoribonuclease Las1 for specific RNA cleavage.Proceedings of the National Academy of Sciences of the United States of America · 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
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3 authors.
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Abstract
Pcf11 and Clp1 are subunits of cleavage factor IA (CFIA), an essential polyadenylation factor in Saccahromyces cerevisiae. We have determined the structure of a ternary complex of Clp1 together with ATP and the Clp1-binding region of Pcf11. Clp1 contains three domains, a small N-terminal beta sandwich domain, a C-terminal domain containing a novel alpha/beta-fold and a central domain that binds ATP. The arrangement of the nucleotide binding site is similar to that observed in SIMIBI-class ATPase subunits found in other multisubunit macromolecular complexes. However, despite this similarity, nucleotide hydrolysis does not occur. The Pcf11 binding site is also located in the central domain where three highly conserved residues in Pcf11 mediate many of the protein-protein interactions. We propose that this conserved Clp1-Pcf11 interaction is responsible for maintaining a tight coupling between the Clp1 nucleotide binding subunit and the other components of the polyadenylation machinery. Moreover, we suggest that this complex represents a stabilized ATP bound form of Clp1 that requires the participation of other non-CFIA processing factors in order to initiate timely ATP hydrolysis during 3' end processing.
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