ArticleProceedings of the National Academy of Sciences of the United States of America2005
A bifunctional DNA repair protein from Ferroplasma acidarmanus exhibits O6-alkylguanine-DNA alkyltransferase and endonuclease V activities.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 39 citations in OpenAlex.
- The DNA Alkyltransferase Family of DNA Repair Proteins: Common Mechanisms, Diverse Functions.International journal of molecular sciences · 2023Review
- Archaeal DNA alkylation repair conducted by DNA glycosylase and methyltransferase.Applied microbiology and biotechnology · 2023Review
- Biochemical and mutational studies of an endonuclease V from the hyperthermophilic crenarchaeon Sulfolobus islandicus REY15A.World journal of microbiology & biotechnology · 2023Article
- Archaeal DNA Repair Mechanisms.Biomolecules · 2020Review
- New Insights Into DNA Repair Revealed by NucS Endonucleases From Hyperthermophilic Archaea.Frontiers in microbiology · 2020Review
- Crystal structure and MD simulation of mouse EndoV reveal wedge motif plasticity in this inosine-specific endonuclease.Scientific reports · 2016Article
- A novel endonuclease that may be responsible for damaged DNA base repair in Pyrococcus furiosus.Nucleic acids research · 2015Article
- Endonuclease V: an unusual enzyme for repair of DNA deamination.Cellular and molecular life sciences : CMLS · 2013Review
- Endonuclease V cleaves at inosines in RNA.Nature communications · 2013Article
- The human homolog of Escherichia coli endonuclease V is a nucleolar protein with affinity for branched DNA structures.PloS one · 2012Article
- Multifaceted roles of alkyltransferase and related proteins in DNA repair, DNA damage, resistance to chemotherapy, and research tools.Chemical research in toxicology · 2011Review
- Alkyltransferase-like proteins: molecular switches between DNA repair pathways.Cellular and molecular life sciences : CMLS · 2010Review
- Article
- Molybdate treatment and sulfate starvation decrease ATP and DNA levels in Ferroplasma acidarmanu.Archaea (Vancouver, B.C.) · 2008Article
- Differential inactivation of polymorphic variants of human O6-alkylguanine-DNA alkyltransferase.Biochemical pharmacology · 2008Article
- Review
- Characterization of an ATP-dependent DNA ligase from the acidophilic archaeon "Ferroplasma acidarmanus" Fer1.Extremophiles : life under extreme conditions · 2007Article
- Direct reversal of DNA alkylation damage.Chemical reviews · 2006Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
A recently discovered DNA repair protein of 303 aa from the archaeal organism Ferroplasma acidarmanus was studied. This protein (AGTendoV) consists of a fusion of the C-terminal active site domain of O(6)-alkylguanine-DNA alkyltransferase (AGT) with an endonuclease V domain. The AGTendoV recombinant protein expressed in Escherichia coli and purified to homogeneity repaired O(6)-methylguanine lesions in DNA via alkyl transfer action despite the complete absence of the N-terminal domain and some differences in key active site residues present in known AGTs. The AGTendoV recombinant protein also cleaved DNA substrates that contained the deaminated bases uracil, hypoxanthine, or xanthine in a similar manner to E. coli endonuclease V. Expression of AGTendoV in E. coli GWR109, a strain that lacks endogenous AGT activity, protected against both the killing and mutagenic activity of N-methyl-N'-nitro-N-nitrosoguanidine and was more effective in preventing mutations than human alkyltransferase, suggesting that the endonuclease V activity may also repair a promutagenic lesion produced by this alkylating agent. Expression of AGTendoV in a DNA repair-deficient E. coli nfi(-)alkA(-) strain protected from spontaneous mutations arising in saturated cultures and restored the mutation frequency to that found in the nfi(+) alkA(+) strain. These results demonstrate the physiological occurrence of two completely different but functional DNA repair activities in a single polypeptide chain.
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