ArticleNucleic acids research2013
Archaeal β-CASP ribonucleases of the aCPSF1 family are orthologs of the eukaryal CPSF-73 factor.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 49 citations in OpenAlex.
- Asgard archaea: have we found our microbial ancestors?The EMBO journal · 2026Review
- Archaeal RNA processing and regulation: expanding the functional landscape.Microbiology and molecular biology reviews : MMBR · 2025Review
- The Thermococcales as a model system: historical perspectives and emerging tools.Journal of bacteriology · 2025Review
- Toward structural understanding of eukaryotic transcription elongation.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2025Review
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- Endonucleolytic processing plays a critical role in the maturation of ribosomal RNA inRNA biology · 2023Article
- aCPSF1 cooperates with terminator U-tract to dictate archaeal transcription termination efficacy.eLife · 2021Article
- The Archaeal Transcription Termination Factor aCPSF1 is a Robust Phylogenetic Marker for Archaeal Taxonomy.Microbiology spectrum · 2021Article
- Promoter-proximal elongation regulates transcription in archaea.Nature communications · 2021Article
- On the Cutting Edge: Regulation and Therapeutic Potential of the mRNA 3' End Nuclease.Trends in biochemical sciences · 2021Review
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- Studies with recombinant U7 snRNP demonstrate that CPSF73 is both an endonuclease and a 5'-3' exonuclease.RNA (New York, N.Y.) · 2020Article
- Archaeal transcription.Transcription · 2020Review
- The conserved ribonuclease aCPSF1 triggers genome-wide transcription termination of Archaea via a 3'-end cleavage mode.Nucleic acids research · 2020Article
- RNA processing machineries in Archaea: the 5'-3' exoribonuclease aRNase J of the β-CASP family is engaged specifically with the helicase ASH-Ski2 and the 3'-5' exoribonucleolytic RNA exosome machinery.Nucleic acids research · 2020Article
- FttA is a CPSF73 homologue that terminates transcription in Archaea.Nature microbiology · 2020Article
- Plant Ribonuclease J: An Essential Player in Maintaining Chloroplast RNA Quality Control for Gene Expression.Plants (Basel, Switzerland) · 2020Review
- The torpedo effect in Bacillus subtilis: RNase J1 resolves stalled transcription complexes.The EMBO journal · 2020Article
- The Arabidopsis chloroplast RNase J displays both exo- and robust endonucleolytic activities.Plant molecular biology · 2019Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial RNase J and eukaryal cleavage and polyadenylation specificity factor (CPSF-73) are members of the β-CASP family of ribonucleases involved in mRNA processing and degradation. Here we report an in-depth phylogenomic analysis that delineates aRNase J and archaeal CPSF (aCPSF) as distinct orthologous groups and establishes their repartition in 110 archaeal genomes. The aCPSF1 subgroup, which has been inherited vertically and is strictly conserved, is characterized by an N-terminal extension with two K homology (KH) domains and a C-terminal motif involved in dimerization of the holoenzyme. Pab-aCPSF1 (Pyrococcus abyssi homolog) has an endoribonucleolytic activity that preferentially cleaves at single-stranded CA dinucleotides and a 5'-3' exoribonucleolytic activity that acts on 5' monophosphate substrates. These activities are the same as described for the eukaryotic cleavage and polyadenylation factor, CPSF-73, when engaged in the CPSF complex. The N-terminal KH domains are important for endoribonucleolytic cleavage at certain specific sites and the formation of stable high molecular weight ribonucleoprotein complexes. Dimerization of Pab-aCPSF is important for exoribonucleolytic activity and RNA binding. Altogether, our results suggest that aCPSF1 performs an essential function and that an enzyme with similar activities was present in the last common ancestor of Archaea and Eukarya.
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