ArticleOpen biology2012
Crystal structure of Caulobacter crescentus polynucleotide phosphorylase reveals a mechanism of RNA substrate channelling and RNA degradosome assembly.
Article in Open biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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44 citing papers in PubMed, 66 citations in OpenAlex.
- Structural insights into RNA recognition by theProceedings of the National Academy of Sciences of the United States of America · 2026Article
- BR-bodies facilitate adaptive responses and survival during copper stress in Caulobacter crescentus.The Journal of biological chemistry · 2025Article
- Human polynucleotide phosphorylase in mitochondrial RNA metabolism.Bioscience reports · 2025Review
- A multi-dentate, cooperative interaction between endo- and exo-ribonucleases within the bacterial RNA degradosome.Nucleic acids research · 2025Article
- Selective inhibition of Mycobacterium tuberculosis GpsI unveils a novel strategy to target the RNA metabolism.Nucleic acids research · 2025Article
- RNA sculpting by the primordial Helix-clasp-Helix-Strand-Loop (HcH-SL) motif enforces chemical recognition enabling diverse KH domain functions.The Journal of biological chemistry · 2025Review
- Critical functions and key interactions mediated by the RNase E scaffolding domain in Pseudomonas aeruginosa.PLoS genetics · 2025Article
- Structural insights into human PNPase in health and disease.Nucleic acids research · 2025Article
- Pathological PNPase variants with altered RNA binding and degradation activity affect the phenotype of bacterial and human cell models.NAR molecular medicine · 2025Article
- pyRBDome: a comprehensive computational platform for enhancing RNA-binding proteome data.Life science alliance · 2024Article
- Structural insights into RNA cleavage by a novel family of bacterial RNases.Nucleic acids research · 2024Article
- Structural insights into RNA cleavage by a novel family of bacterial RNases.Research square · 2023Article
- RNase E biomolecular condensates stimulate PNPase activity.Scientific reports · 2023Article
- Dimeric assembly of human Suv3 helicase promotes its RNA unwinding function in mitochondrial RNA degradosome for RNA decay.Protein science : a publication of the Protein Society · 2022Article
- Activity and Function in Human Cells of the Evolutionary Conserved Exonuclease Polynucleotide Phosphorylase.International journal of molecular sciences · 2022Review
- KH domain proteins: Another family of bacterial RNA matchmakers?Molecular microbiology · 2022Review
- Polynucleotide phosphorylase and RNA helicase CshA cooperate inRNA biology · 2021Article
- A cooperative PNPase-Hfq-RNA carrier complex facilitates bacterial riboregulation.Molecular cell · 2021Article
- Computational evolution of an RNA-binding protein towards enhanced oxidized-RNA binding.Computational and structural biotechnology journal · 2020Article
- The Bacterial Counterparts of the Eukaryotic Exosome: An Evolutionary Perspective.Methods in molecular biology (Clifton, N.J.) · 2020Review
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Polynucleotide phosphorylase (PNPase) is an exoribonuclease that cleaves single-stranded RNA substrates with 3'-5' directionality and processive behaviour. Its ring-like, trimeric architecture creates a central channel where phosphorolytic active sites reside. One face of the ring is decorated with RNA-binding K-homology (KH) and S1 domains, but exactly how these domains help to direct the 3' end of single-stranded RNA substrates towards the active sites is an unsolved puzzle. Insight into this process is provided by our crystal structures of RNA-bound and apo Caulobacter crescentus PNPase. In the RNA-free form, the S1 domains adopt a 'splayed' conformation that may facilitate capture of RNA substrates. In the RNA-bound structure, the three KH domains collectively close upon the RNA and direct the 3' end towards a constricted aperture at the entrance of the central channel. The KH domains make non-equivalent interactions with the RNA, and there is a marked asymmetry within the catalytic core of the enzyme. On the basis of these data, we propose that structural non-equivalence, induced upon RNA binding, helps to channel substrate to the active sites through mechanical ratcheting. Structural and biochemical analyses also reveal the basis for PNPase association with RNase E in the multi-enzyme RNA degradosome assembly of the α-proteobacteria.
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