ArticleNucleic acids research2012
The interaction of Pcf11 and Clp1 is needed for mRNA 3'-end formation and is modulated by amino acids in the ATP-binding site.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 34 citations in OpenAlex.
- Mechanisms of transcription termination across the coding and noncoding loci of the genome.Nature reviews. Molecular cell biology · 2026Review
- hnRNPUL1 has a dead polynucleotide kinase domain that regulates RNA and protein interactions.iScience · 2026Article
- Polyadenylation Complex CFII Recognizes Downstream Cis-element for Pre-mRNA Polyadenylation Through Interaction with an RNA-Binding Protein in Arabidopsis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Article
- Systematic Analysis of Diverse Polynucleotide Kinase Clp1 Family Proteins in Eukaryotes: Three Unique Clp1 Proteins of Trypanosoma brucei.Journal of molecular evolution · 2023Article
- 3'-End Processing of Eukaryotic mRNA: Machinery, Regulation, and Impact on Gene Expression.Annual review of biochemistry · 2023Review
- Article
- 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
- Reconstitution of mammalian cleavage factor II involved in 3' processing of mRNA precursors.RNA (New York, N.Y.) · 2018Article
- RNA Polymerase II Transcription Attenuation at the Yeast DNA Repair Gene,G3 (Bethesda, Md.) · 2018Article
- 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
- The Nrd1-like protein Seb1 coordinates cotranscriptional 3' end processing and polyadenylation site selection.Genes & development · 2016Article
- An investigation into the role of ATP in the mammalian pre-mRNA 3' cleavage reaction.Biochimie · 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
- The regulatory role of Pcf11-similar-4 (PCFS4) in Arabidopsis development by genome-wide physical interactions with target loci.BMC genomics · 2013Article
- Kaposi's sarcoma-associated herpesvirus ORF57 protein: exploiting all stages of viral mRNA processing.Viruses · 2013Review
- Article
- Chtop is a component of the dynamic TREX mRNA export complex.The EMBO journal · 2013Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
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Abstract
Polyadenylation of eukaryotic mRNAs contributes to stability, transport and translation, and is catalyzed by a large complex of conserved proteins. The Pcf11 subunit of the yeast CF IA factor functions as a scaffold for the processing machinery during the termination and polyadenylation of transcripts. Its partner, Clp1, is needed for mRNA processing, but its precise molecular role has remained enigmatic. We show that Clp1 interacts with the Cleavage-Polyadenylation Factor (CPF) through its N-terminal and central domains, and thus provides cross-factor connections within the processing complex. Clp1 is known to bind ATP, consistent with the reported RNA kinase activity of human Clp1. However, substitution of conserved amino acids in the ATP-binding site did not affect cell growth, suggesting that the essential function of yeast Clp1 does not involve ATP hydrolysis. Surprisingly, non-viable mutations predicted to displace ATP did not affect ATP binding but disturbed the Clp1-Pcf11 interaction. In support of the importance of this interaction, a mutation in Pcf11 that disrupts the Clp1 contact caused defects in growth, 3'-end processing and transcription termination. These results define Clp1 as a bridge between CF IA and CPF and indicate that the Clp1-Pcf11 interaction is modulated by amino acids in the conserved ATP-binding site of Clp1.
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Registered trials
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