ArticleNucleic acids research2016
The oligomeric architecture of the archaeal exosome is important for processive and efficient RNA degradation.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Catalytic activities, molecular connections, and biological functions of plant RNA exosome complexes.The Plant cell · 2022Review
- iCLIP analysis of RNA substrates of the archaeal exosome.BMC genomics · 2020Article
- Molecular basis of the selective processing of short mRNA substrates by the DcpS mRNA decapping enzyme.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Enzymatic Analysis of Reconstituted Archaeal Exosomes.Methods in molecular biology (Clifton, N.J.) · 2020Article
- RNA degradation by the plant RNA exosome involves both phosphorolytic and hydrolytic activities.Nature communications · 2017Article
- A synergistic network of interactions promotes the formation of in vitro processing bodies and protects mRNA against decapping.Nucleic acids research · 2017Article
- Changes in conformational equilibria regulate the activity of the Dcp2 decapping enzyme.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The Rrp4-exosome complex recruits and channels substrate RNA by a unique mechanism.Nature chemical biology · 2017Article
- A general method for rapid and cost-efficient large-scale production of 5' capped RNA.RNA (New York, N.Y.) · 2016Article
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Authors and funding
4 authors.
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Abstract
The exosome plays an important role in RNA degradation and processing. In archaea, three Rrp41:Rrp42 heterodimers assemble into a barrel like structure that contains a narrow RNA entrance pore and a lumen that contains three active sites. Here, we demonstrate that this quaternary structure of the exosome is important for efficient RNA degradation. We find that the entrance pore of the barrel is required for nM substrate affinity. This strong interaction is crucial for processive substrate degradation and prevents premature release of the RNA from the enzyme. Using methyl TROSY NMR techniques, we establish that the 3' end of the substrate remains highly flexible inside the lumen. As a result, the RNA jumps between the three active sites that all equally participate in substrate degradation. The RNA jumping rate is, however, much faster than the cleavage rate, indicating that not all active site:substrate encounters result in catalysis. Enzymatic turnover therefore benefits from the confinement of the active sites and substrate in the lumen, which ensures that the RNA is at all times bound to one of the active sites. The evolution of the exosome into a hexameric complex and the optimization of its catalytic efficiency were thus likely co-occurring events.
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