ArticleJournal of molecular biology2012
Substrate-dependent millisecond domain motions in DNA polymerase β.
Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 23 citations in OpenAlex.
- The S180R Human Germline Variant of DNA Polymerase β Is a Low Fidelity Enzyme with Reduced Flexibility of the Fingers Domain.Biochemistry · 2026Article
- NMR and computational methods for molecular resolution of allosteric pathways in enzyme complexes.Biophysical reviews · 2020Review
- I260Q DNA polymerase β highlights precatalytic conformational rearrangements critical for fidelity.Nucleic acids research · 2018Article
- The nature of the DNA substrate influences pre-catalytic conformational changes of DNA polymerase β.The Journal of biological chemistry · 2018Article
- Transitions in DNA polymerase β μs-ms dynamics related to substrate binding and catalysis.Nucleic acids research · 2018Article
- Role of Conformational Motions in Enzyme Function: Selected Methodologies and Case Studies.Catalysts (Basel, Switzerland) · 2016Article
- Using NMR spectroscopy to elucidate the role of molecular motions in enzyme function.Progress in nuclear magnetic resonance spectroscopy · 2016Review
- Induced Fit in the Selection of Correct versus Incorrect Nucleotides by DNA Polymerase β.Biochemistry · 2016Article
- Substrate-induced DNA polymerase β activation.The Journal of biological chemistry · 2014Article
- Real-time surface plasmon resonance study of biomolecular interactions between polymerase and bulky mutagenic DNA lesions.Chemical research in toxicology · 2014Article
- Direct correlation of DNA binding and single protein domain motion via dual illumination fluorescence microscopy.Nano letters · 2014Article
- Article
- Optimal and variant metal-ion routes in DNA polymerase β's conformational pathways.Journal of the American Chemical Society · 2014Article
- The E295K cancer variant of human polymerase β favors the mismatch conformational pathway during nucleotide selection.The Journal of biological chemistry · 2013Article
- NMR paves the way for atomic level descriptions of sparsely populated, transiently formed biomolecular conformers.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Mapping the structural and dynamical features of multiple p53 DNA binding domains: insights into loop 1 intrinsic dynamics.PloS one · 2013Article
- "Gate-keeper" residues and active-site rearrangements in DNA polymerase μ help discriminate non-cognate nucleotides.PLoS computational biology · 2013Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
DNA polymerase β (Pol β) is a 39-kDa enzyme that performs the vital cellular function of repairing damaged DNA. Mutations in Pol β have been linked to various cancers, and these mutations are further correlated with altered Pol β enzymatic activity. The fidelity of correct nucleotide incorporation into damaged DNA is essential for Pol β repair function, and several studies have implicated conformational changes in Pol β as a determinant of this repair fidelity. In this work, the rate constants for domain motions in Pol β have been determined by solution NMR relaxation dispersion for the apo and substrate-bound, binary forms of Pol β. In apo Pol β, molecular motions, primarily isolated to the DNA lyase domain, are observed to occur at 1400 s(-1). Additional analysis suggests that these motions allow apo Pol β to sample a conformation similar to the gapped DNA-substrate-bound form. Upon binding DNA, these lyase domain motions are significantly quenched, whereas evidence for conformational motions in the polymerase domain becomes apparent. These NMR studies suggest an alteration in the dynamic landscape of Pol β due to substrate binding. Moreover, a number of the flexible residues identified in this work are also the location of residues, which upon mutation lead to cancer phenotypes in vivo, which may be due to the intimate role of protein motions in Pol β fidelity.
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