ArticleThe Biochemical journal2016
The first crystal structure of human RNase 6 reveals a novel substrate-binding and cleavage site arrangement.
Article in The Biochemical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Bacterial RNA sensing by TLR8 requires RNase 6 processing and is inhibited by RNA 2'O-methylation.EMBO reports · 2024Article
- Nucleotide modifications enable rational design of TLR7-selective ligands by blocking RNase cleavage.The Journal of experimental medicine · 2024Article
- A Common Polymorphism inInternational journal of molecular sciences · 2024Article
- Functional Insight into hTRIR.Current molecular medicine · 2024Article
- Selective cleavage of ncRNA and antiviral activity by RNase2/EDN in THP1-induced macrophages.Cellular and molecular life sciences : CMLS · 2022Article
- Structure-Based Design of an RNase Chimera for Antimicrobial Therapy.International journal of molecular sciences · 2021Article
- Insights into Structural and Dynamical Changes Experienced by Human RNase 6 upon Ligand Binding.Biochemistry · 2020Article
- Functional roles of the human ribonuclease A superfamily in RNA metabolism and membrane receptor biology.Molecular aspects of medicine · 2019Review
- Biological Activities of Secretory RNases: Focus on Their Oligomerization to Design Antitumor Drugs.Frontiers in immunology · 2019Review
- Human Antimicrobial RNases Inhibit Intracellular Bacterial Growth and Induce Autophagy in Mycobacteria-Infected Macrophages.Frontiers in immunology · 2019Article
- Nucleotide substrate binding characterization in human pancreatic-type ribonucleases.PloS one · 2019Article
- Evolutionary Trends in RNA Base Selectivity Within the RNase A Superfamily.Frontiers in pharmacology · 2019Article
- Immune Modulation by Human Secreted RNases at the Extracellular Space.Frontiers in immunology · 2018Review
- Human Skin RNases Offer Dual Protection against Invading Bacteria.Frontiers in microbiology · 2017Article
- Insights into the Antimicrobial Mechanism of Action of Human RNase6: Structural Determinants for Bacterial Cell Agglutination and Membrane Permeation.International journal of molecular sciences · 2016Article
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Authors and funding
7 authors.
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Abstract
Human RNase 6 is a cationic secreted protein that belongs to the RNase A superfamily. Its expression is induced in neutrophils and monocytes upon bacterial infection, suggesting a role in host defence. We present here the crystal structure of RNase 6 obtained at 1.72 Å (1 Å=0.1 nm) resolution, which is the first report for the protein 3D structure and thereby setting the basis for functional studies. The structure shows an overall kidney-shaped globular fold shared with the other known family members. Three sulfate anions bound to RNase 6 were found, interacting with residues at the main active site (His(15), His(122) and Gln(14)) and cationic surface-exposed residues (His(36), His(39), Arg(66) and His(67)). Kinetic characterization, together with prediction of protein-nucleotide complexes by molecular dynamics, was applied to analyse the RNase 6 substrate nitrogenous base and phosphate selectivity. Our results reveal that, although RNase 6 is a moderate catalyst in comparison with the pancreatic RNase type, its structure includes lineage-specific features that facilitate its activity towards polymeric nucleotide substrates. In particular, enzyme interactions at the substrate 5' end can provide an endonuclease-type cleavage pattern. Interestingly, the RNase 6 crystal structure revealed a novel secondary active site conformed by the His(36)-His(39) dyad that facilitates the polynucleotide substrate catalysis.
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