ArticleNucleic acids research2006
A novel DNA damage recognition protein in Schizosaccharomyces pombe.
Article in Nucleic acids research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 28 citations in OpenAlex.
- Bracken Fern Carcinogen, Ptaquiloside, Forms a GuanineJournal of agricultural and food chemistry · 2025Article
- Development and Application of a Slot-Blot Assay Using the Damage Sensing Protein Atl1 to Detect and QuantifyToxics · 2024Article
- The DNA Alkyltransferase Family of DNA Repair Proteins: Common Mechanisms, Diverse Functions.International journal of molecular sciences · 2023Review
- Mass Spectrometric Analysis of the Active Site Tryptic Peptide of RecombinantChemical research in toxicology · 2023Article
- Mutational Analysis of N-Ethyl-N-Nitrosourea (ENU) in the Fission YeastG3 (Bethesda, Md.) · 2020Article
- DNA repair by reversal of DNA damage.Cold Spring Harbor perspectives in biology · 2013Review
- Alkyltransferase-like protein (Atl1) distinguishes alkylated guanines for DNA repair using cation-π interactions.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Lesion-specific DNA-binding and repair activities of human O⁶-alkylguanine DNA alkyltransferase.Nucleic acids research · 2012Article
- Atl1 regulates choice between global genome and transcription-coupled repair of O(6)-alkylguanines.Molecular cell · 2012Article
- On the Use of Gene Ontology Annotations to Assess Functional Similarity among Orthologs and Paralogs: A Short Report.PLoS computational biology · 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
- Alkyltransferase-like protein (eATL) prevents mismatch repair-mediated toxicity induced by O6-alkylguanine adducts in Escherichia coli.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Molecular mechanisms of the whole DNA repair system: a comparison of bacterial and eukaryotic systems.Journal of nucleic acids · 2010Article
- Structural basis of O6-alkylguanine recognition by a bacterial alkyltransferase-like DNA repair protein.The Journal of biological chemistry · 2010Article
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Toxic and mutagenic O6-alkylguanine adducts in DNA are repaired by O6-alkylguanine-DNA alkyltransferases (MGMT) by transfer of the alkyl group to a cysteine residue in the active site. Comparisons in silico of prokaryotes and lower eukaryotes reveal the presence of a group of proteins [alkyltransferase-like (ATL) proteins] showing amino acid sequence similarity to MGMT, but where the cysteine at the putative active site is replaced by tryptophan. To examine whether ATL proteins play a role in the biological effects of alkylating agents, we inactivated the gene, referred to as atl1+, in Schizosaccharomyces pombe, an organism that does not possess a functional MGMT homologue. The mutants are substantially more susceptible to the toxic effects of the methylating agents, N-methyl-N-nitrosourea, N-methyl-N'nitro-N-nitrosoguanidine and methyl methanesulfonate and longer chain alkylating agents including N-ethyl-N-nitrosourea, ethyl methanesulfonate, N-propyl-N-nitrosourea and N-butyl-N-nitrosourea. Purified Atl1 protein does not transfer methyl groups from O6-methylguanine in [3H]-methylated DNA but reversibly inhibits methyl transfer by human MGMT. Atl1 binds to short single-stranded oligonucleotides containing O6-methyl, -benzyl, -4-bromothenyl or -hydroxyethyl-guanine but does not remove the alkyl group or base and does not cleave the oligonucleotide in the region of the lesion. This suggests that Atl1 acts by binding to O6-alkylguanine lesions and signalling them for processing by other DNA repair pathways. This is the first report describing an activity that protects S.pombe against the toxic effects of O6-alkylguanine adducts and the biological function of a family of proteins that is widely found in prokaryotes and lower eukaryotes.
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