ArticleThe Journal of biological chemistry2015
Roles of Residues Arg-61 and Gln-38 of Human DNA Polymerase η in Bypass of Deoxyguanosine and 7,8-Dihydro-8-oxo-2'-deoxyguanosine.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 39 citations in OpenAlex.
- Human TLS DNA polymerase: saviors or threats under replication stress?Molecular and cellular biochemistry · 2025Review
- Connecting dots between nucleotide biosynthesis and DNA lesion repair/bypass in cancer.Bioscience reports · 2024Review
- Novel insights into the role of translesion synthesis polymerase in DNA incorporation and bypass of 5-fluorouracil in colorectal cancer.Nucleic acids research · 2024Article
- Replication Bypass of theBiochemistry · 2024Article
- Incorporation of inosine into DNA by human polymerase eta (Polη): kinetics of nucleotide misincorporation and structural basis for the mutagenicity.The Biochemical journal · 2023Article
- Article
- Site-Specific 5-Formyl Cytosine Mediated DNA-Histone Cross-Links: Synthesis and Polymerase Bypass by Human DNA Polymerase η.Angewandte Chemie (International ed. in English) · 2021Article
- Translesion Synthesis Past 5-Formylcytosine-Mediated DNA-Peptide Cross-Links by hPolη Is Dependent on the Local DNA Sequence.Biochemistry · 2021Article
- Quaternary structural diversity in eukaryotic DNA polymerases: monomeric to multimeric form.Current genetics · 2020Review
- Mutagenesis mechanism of the major oxidative adenine lesion 7,8-dihydro-8-oxoadenine.Nucleic acids research · 2020Article
- Impact of 1,The Journal of biological chemistry · 2020Article
- Human DNA polymerase η has reverse transcriptase activity in cellular environments.The Journal of biological chemistry · 2019Article
- Structural basis for the bypass of the major oxaliplatin-DNA adducts by human DNA polymerase η.The Biochemical journal · 2019Article
- The active site residues Gln55 and Arg73 play a key role in DNA damage bypass by S. cerevisiae Pol η.Scientific reports · 2018Article
- Human DNA polymerase η accommodates RNA for strand extension.The Journal of biological chemistry · 2017Article
- Increased Processivity, Misincorporation, and Nucleotide Incorporation Efficiency in Sulfolobus solfataricus Dpo4 Thumb Domain Mutants.Applied and environmental microbiology · 2017Article
- Translesion DNA polymerases in eukaryotes: what makes them tick?Critical reviews in biochemistry and molecular biology · 2017Review
- Effects of Active Site Mutations on Specificity of Nucleobase Binding in Human DNA Polymerase η.The journal of physical chemistry. B · 2017Article
- Excessive Reactive Oxygen Species and Exotic DNA Lesions as an Exploitable Liability.Biochemistry · 2016Review
- Capture of a third Mg²⁺ is essential for catalyzing DNA synthesis.Science (New York, N.Y.) · 2016Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Like the other Y-family DNA polymerases, human DNA polymerase η (hpol η) has relatively low fidelity and is able to tolerate damage during DNA synthesis, including 7,8-dihydro-8-oxo-2'-deoxyguanosine (8-oxoG), one of the most abundant DNA lesions in the genome. Crystal structures show that Arg-61 and Gln-38 are located near the active site and may play important roles in the fidelity and efficiency of hpol η. Site-directed mutagenesis was used to replace these side chains either alone or together, and the wild type or mutant proteins were purified and tested by replicating DNA past deoxyguanosine (G) or 8-oxoG. The catalytic activity of hpol η was dramatically disrupted by the R61M and Q38A/R61A mutations, as opposed to the R61A and Q38A single mutants. Crystal structures of hpol η mutant ternary complexes reveal that polarized water molecules can mimic and partially compensate for the missing side chains of Arg-61 and Gln-38 in the Q38A/R61A mutant. The combined data indicate that the positioning and positive charge of Arg-61 synergistically contribute to the nucleotidyl transfer reaction, with additional influence exerted by Gln-38. In addition, gel filtration chromatography separated multimeric and monomeric forms of wild type and mutant hpol η, indicating the possibility that hpol η forms multimers in vivo.
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