ArticleNucleic acids research2017
Structure of acid deoxyribonuclease.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 32 citations in OpenAlex.
- Article
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- Advancements in Aptamer-Driven DNA Nanostructures for Precision Drug Delivery.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Review
- Structural and mechanistic insights into disease-associated endolysosomal exonucleases PLD3 and PLD4.Structure (London, England : 1993) · 2024Article
- Artificial Intelligence-Guided Gut-Microenvironment-Triggered Imaging Sensor Reveals Potential Indicators of Parkinson's Disease.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Improving DNA nanostructure stability: A review of the biomedical applications and approaches.International journal of biological macromolecules · 2024Review
- Structural analysis of PLD3 reveals insights into the mechanism of lysosomal 5' exonuclease-mediated nucleic acid degradation.Nucleic acids research · 2024Article
- Mild Heat Treatment and Biopreservatives for Artisanal Raw Milk Cheeses: Reducing Microbial Spoilage and Extending Shelf-Life through Thermisation, Plant Extracts and Lactic Acid Bacteria.Foods (Basel, Switzerland) · 2023Review
- A virus changed my life.Molecular biology of the cell · 2022Article
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- A Role of Epithelial Cells and Virulence Factors in Biofilm Formation by Streptococcus pyogenesInfection and immunity · 2020Article
- Pyronaridine exerts potent cytotoxicity on human breast and hematological cancer cells through induction of apoptosis.PloS one · 2018Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Deoxyribonuclease II (DNase II) is also known as acid deoxyribonuclease because it has optimal activity at the low pH environment of lysosomes where it is typically found in higher eukaryotes. Interestingly, DNase II has also been identified in a few genera of bacteria and is believed to have arisen via horizontal transfer. Here, we demonstrate that recombinant Burkholderia thailandensis DNase II is highly active at low pH in the absence of divalent metal ions, similar to eukaryotic DNase II. The crystal structure of B. thailandensis DNase II shows a dimeric quaternary structure which appears capable of binding double-stranded DNA. Each monomer of B. thailandensis DNase II exhibits a similar overall fold as phospholipase D (PLD), phosphatidylserine synthase (PSS) and tyrosyl-DNA phosphodiesterase (TDP), and conserved catalytic residues imply a similar mechanism. The structural and biochemical data presented here provide insights into the atomic structure and catalytic mechanism of DNase II.
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