ArticleThe Biochemical journal2012
Staphylococcus aureus DinG, a helicase that has evolved into a nuclease.
Article in The Biochemical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 29 citations in OpenAlex.
- Structural and biochemical characterization of a novel DinG containing an endonuclease domain.Cellular and molecular life sciences : CMLS · 2026Article
- The DinG exonuclease acts as a primary quality controller to remove unprocessed ribosomal RNAs.Nucleic acids research · 2026Article
- Modulators of gene amplification alter evolution of antibiotic resistance in Staphylococcus aureus.PLoS genetics · 2025Article
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- A gate-clamp mechanism for ssDNA translocation by DdmD in Vibrio cholerae plasmid defense.Nucleic acids research · 2025Article
- Hallmarks of DNA replication stress responses in Escherichia coli and Bacillus subtilis.FEMS microbiology reviews · 2025Review
- Structure, function and evolution of the bacterial DinG-like proteins.Computational and structural biotechnology journal · 2025Review
- Processing of stalled replication forks in Bacillus subtilis.FEMS microbiology reviews · 2024Review
- CasDinG is a 5'-3' dsDNA and RNA/DNA helicase with three accessory domains essential for type IV CRISPR immunity.Nucleic acids research · 2023Article
- Exploring the G-quadruplex binding and unwinding activity of the bacterial FeS helicase DinG.Scientific reports · 2023Article
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- Positioning Diverse Type IV Structures and Functions Within Class 1 CRISPR-Cas Systems.Frontiers in microbiology · 2021Article
- Type IV CRISPR-Cas systems are highly diverse and involved in competition between plasmids.Nucleic acids research · 2020Article
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- A Look into the Melting Pot: The mecC-Harboring Region Is a Recombination Hot Spot in Staphylococcus stepanovicii.PloS one · 2016Article
- YbiB from Escherichia coli, the Defining Member of the Novel TrpD2 Family of Prokaryotic DNA-binding Proteins.The Journal of biological chemistry · 2015Article
- Genomic, Transcriptomic and Metabolomic Studies of Two Well-Characterized, Laboratory-Derived Vancomycin-Intermediate Staphylococcus aureus Strains Derived from the Same Parent Strain.Antibiotics (Basel, Switzerland) · 2015Article
- Functional genomics of Lactobacillus casei establishment in the gut.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- A highly conserved family of domains related to the DNA-glycosylase fold helps predict multiple novel pathways for RNA modifications.RNA biology · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
DinG (damage inducible gene G) is a bacterial superfamily 2 helicase with 5′→3′ polarity. DinG is related to the XPD (xeroderma pigmentosum complementation group D) helicase family, and they have in common an FeS (iron–sulfur)-binding domain that is essential for the helicase activity. In the bacilli and clostridia, the DinG helicase has become fused with an N-terminal domain that is predicted to be an exonuclease. In the present paper we show that the DinG protein from Staphylococcus aureus lacks an FeS domain and is not a DNA helicase, although it retains DNA-dependent ATP hydrolysis activity. Instead, the enzyme is an active 3′→5′ exonuclease acting on single-stranded DNA and RNA substrates. The nuclease activity can be modulated by mutation of the ATP-binding cleft of the helicase domain, and is inhibited by ATP or ADP, suggesting a modified role for the inactive helicase domain in the control of the nuclease activity. By degrading rather than displacing RNA or DNA strands, the S. aureus DinG nuclease may accomplish the same function as the canonical DinG helicase.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.