ArticleNucleic acids research2012
How an exonuclease decides where to stop in trimming of nucleic acids: crystal structures of RNase T-product complexes.
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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22 citing papers in PubMed, 38 citations in OpenAlex.
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- Molecular insight into the specific enzymatic properties of TREX1 revealing the diverse functions in processing RNA and DNA/RNA hybrids.Nucleic acids research · 2023Article
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- PML and PML-like exonucleases restrict retrotransposons in jawed vertebrates.Nucleic acids research · 2023Article
- Not making the cut: Techniques to prevent RNA cleavage in structural studies of RNase-RNA complexes.Journal of structural biology: X · 2022Review
- Crystal structure and functional properties of the human CCR4-CAF1 deadenylase complex.Nucleic acids research · 2021Article
- Anatomy of noncovalent interactions between the nucleobases or ribose and π-containing amino acids in RNA-protein complexes.Nucleic acids research · 2021Article
- Understanding APE1 cellular functions by the structural preference of exonuclease activities.Computational and structural biotechnology journal · 2021Review
- A dedicated diribonucleotidase resolves a key bottleneck for the terminal step of RNA degradation.eLife · 2019Article
- Bacterial ribonucleases and their roles in RNA metabolism.Critical reviews in biochemistry and molecular biology · 2019Review
- Structural insights into nanoRNA degradation by human Rexo2.RNA (New York, N.Y.) · 2019Article
- Structural basis of small RNA hydrolysis by oligoribonuclease (CpsORN) from Colwellia psychrerythraea strain 34H.Scientific reports · 2019Article
- Structural insights into the duplex DNA processing of TREX2.Nucleic acids research · 2018Article
- Structural basis for overhang excision and terminal unwinding of DNA duplexes by TREX1.PLoS biology · 2018Article
- Examining tRNA 3'-ends inRNA (New York, N.Y.) · 2018Article
- Mismodeled purines: implicit alternates and hidden Hoogsteens.Acta crystallographica. Section D, Structural biology · 2017Article
- Aromatic residues in RNase T stack with nucleobases to guide the sequence-specific recognition and cleavage of nucleic acids.Protein science : a publication of the Protein Society · 2015Article
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5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Exonucleases are key enzymes in the maintenance of genome stability, processing of immature RNA precursors and degradation of unnecessary nucleic acids. However, it remains unclear how exonucleases digest nucleic acids to generate correct end products for next-step processing. Here we show how the exonuclease RNase T stops its trimming precisely. The crystal structures of RNase T in complex with a stem-loop DNA, a GG dinucleotide and single-stranded DNA with different 3'-end sequences demonstrate why a duplex with a short 3'-overhang, a dinucleotide and a ssDNA with a 3'-end C cannot be further digested by RNase T. Several hydrophobic residues in RNase T change their conformation upon substrate binding and induce an active or inactive conformation in the active site that construct a precise machine to determine which substrate should be digested based on its sequence, length and structure. These studies thus provide mechanistic insights into how RNase T prevents over digestion of its various substrates, and the results can be extrapolated to the thousands of members of the DEDDh family of exonucleases.
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