ArticleProceedings of the National Academy of Sciences of the United States of America2015
Creative template-dependent synthesis by human polymerase mu.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
20 citing papers in PubMed, 27 citations in OpenAlex.
- DNA repair and anti-cancer mechanisms in the long-lived bowhead whale.bioRxiv : the preprint server for biology · 2024Article
- DNA polymerase λ Loop1 variant yields unexpected gain-of-function capabilities in nonhomologous end-joining.DNA repair · 2024Article
- For the Better or for the Worse? The Effect of Manganese on the Activity of Eukaryotic DNA Polymerases.International journal of molecular sciences · 2023Review
- Mechanism of genome instability mediated by human DNA polymerase mu misincorporation.Nature communications · 2021Article
- Structural snapshots of human DNA polymerase μ engaged on a DNA double-strand break.Nature communications · 2020Article
- DNA polymerase mu: An inflexible scaffold for substrate flexibility.DNA repair · 2020Review
- Polymerase μ in non-homologous DNA end joining: importance of the order of arrival at a double-strand break in a purified system.Nucleic acids research · 2020Article
- DNA polymerase β nucleotide-stabilized template misalignment fidelity depends on local sequence context.The Journal of biological chemistry · 2020Article
- Structure and function relationships in mammalian DNA polymerases.Cellular and molecular life sciences : CMLS · 2020Review
- Unexpected behavior of DNA polymerase Mu opposite template 8-oxo-7,8-dihydro-2'-guanosine.Nucleic acids research · 2019Article
- Structural evidence for an inThe Journal of biological chemistry · 2019Article
- Article
- A ubiquitin-like domain is required for stabilizing the N-terminal ATPase module of human SMCHD1.Communications biology · 2019Article
- Translesion and Repair DNA Polymerases: Diverse Structure and Mechanism.Annual review of biochemistry · 2018Review
- Polμ tumor variants decrease the efficiency and accuracy of NHEJ.Nucleic acids research · 2017Article
- Structural accommodation of ribonucleotide incorporation by the DNA repair enzyme polymerase Mu.Nucleic acids research · 2017Article
- Time-lapse crystallography snapshots of a double-strand break repair polymerase in action.Nature communications · 2017Article
- Break-induced replication links microsatellite expansion to complex genome rearrangements.BioEssays : news and reviews in molecular, cellular and developmental biology · 2017Review
- DNA polymerase β uses its lyase domain in a processive search for DNA damage.Nucleic acids research · 2017Article
- Essential role for polymerase specialization in cellular nonhomologous end joining.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Among the many proteins used to repair DNA double-strand breaks by nonhomologous end joining (NHEJ) are two related family X DNA polymerases, Pol λ and Pol µ. Which of these two polymerases is preferentially used for filling DNA gaps during NHEJ partly depends on sequence complementarity at the break, with Pol λ and Pol µ repairing complementary and noncomplementary ends, respectively. To better understand these substrate preferences, we present crystal structures of Pol µ on a 2-nt gapped DNA substrate, representing three steps of the catalytic cycle. In striking contrast to Pol λ, Pol µ "skips" the first available template nucleotide, instead using the template base at the 5' end of the gap to direct nucleotide binding and incorporation. This remarkable divergence from canonical 3'-end gap filling is consistent with data on end-joining substrate specificity in cells, and provides insights into polymerase substrate choices during NHEJ.
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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.