ArticleArchaea (Vancouver, B.C.)2012
Crystal structure of a 9-subunit archaeal exosome in pre-catalytic states of the phosphorolytic reaction.
Article in Archaea (Vancouver, B.C.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 21 citations in OpenAlex.
- Loop-mediated regulation and base flipping drive RNA cleavage by human mitochondrial PNPase.Nucleic acids research · 2025Article
- Structural Insights into the Rrp4 Subunit from the Crystal Structure of theBiomolecules · 2024Article
- Catalytic activities, molecular connections, and biological functions of plant RNA exosome complexes.The Plant cell · 2022Review
- Article
- RNA degradation by the plant RNA exosome involves both phosphorolytic and hydrolytic activities.Nature communications · 2017Article
- Inhibition of homologous phosphorolytic ribonucleases by citrate may represent an evolutionarily conserved communicative link between RNA degradation and central metabolism.Nucleic acids research · 2017Article
- CryoEM structure of yeast cytoplasmic exosome complex.Cell research · 2016Article
- The oligomeric architecture of the archaeal exosome is important for processive and efficient RNA degradation.Nucleic acids research · 2016Article
- Discrimination of RNA from DNA by polynucleotide phosphorylase.Biochemistry · 2013Article
- The archaeal exosome: identification and quantification of site-specific motions that correlate with cap and RNA binding.Angewandte Chemie (International ed. in English) · 2013Article
- mRNA fate: Life and death of the mRNA in the cytoplasm.RNA biology · 2013Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The RNA exosome is an important protein complex that functions in the 3' processing and degradation of RNA in archaeal and eukaryotic organisms. The archaeal exosome is functionally similar to bacterial polynucleotide phosphorylase (PNPase) and RNase PH enzymes as it uses inorganic phosphate (Pi) to processively cleave RNA substrates releasing nucleoside diphosphates. To shed light on the mechanism of catalysis, we have determined the crystal structures of mutant archaeal exosome in complex with either Pi or with both RNA and Pi at resolutions of 1.8 Å and 2.5 Å, respectively. These structures represent views of precatalytic states of the enzyme and allow the accurate determination of the substrate binding geometries. In the structure with both Pi and RNA bound, the Pi closely approaches the phosphate of the 3'-end nucleotide of the RNA and is in a perfect position to perform a nucleophilic attack. The presence of negative charge resulting from the close contacts between the phosphates appears to be neutralized by conserved positively charged residues in the active site of the archaeal exosome. The high degree of structural conservation between the archaeal exosome and the PNPase including the requirement for divalent metal ions for catalysis is discussed.
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Registered trials
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