ArticleProceedings of the National Academy of Sciences of the United States of America2013
Structure-function analysis of ribonucleotide bypass by B family DNA replicases.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 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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Who cites it
34 citing papers in PubMed, 50 citations in OpenAlex.
- Emerging roles of RNA:DNA hybrid regulation by mammalian ribonuclease H2 in replication stress and cancer.Journal of cell science · 2025Review
- Uridine Embedded within DNA is Repaired by Uracil DNA Glycosylase via a Mechanism Distinct from That of Ribonuclease H2.Journal of the American Chemical Society · 2025Article
- Untargeted Mutation Triggered by Ribonucleoside Embedded in DNA.International journal of molecular sciences · 2024Article
- Detection of ribonucleotides embedded in DNA by Nanopore sequencing.Communications biology · 2024Article
- DNA polymerase ε harmonizes topological states and R-loops formation to maintain genome integrity in Arabidopsis.Nature communications · 2023Article
- Evaluation of repair activity by quantification of ribonucleotides in the genome.Genes to cells : devoted to molecular & cellular mechanisms · 2021Article
- High Flexibility of RNaseH2 Catalytic Activity with Respect to Non-Canonical DNA Structures.International journal of molecular sciences · 2021Article
- Mechanisms of damage tolerance and repair during DNA replication.Nucleic acids research · 2021Review
- One, No One, and One Hundred Thousand: The Many Forms of Ribonucleotides in DNA.International journal of molecular sciences · 2020Review
- Bypass of the Major Alkylative DNA Lesion by Human DNA Polymerase η.Molecules (Basel, Switzerland) · 2019Article
- RNase H activities counteract a toxic effect of Polymerase η in cells replicating with depleted dNTP pools.Nucleic acids research · 2019Article
- Human DNA polymerase η has reverse transcriptase activity in cellular environments.The Journal of biological chemistry · 2019Article
- A cancer-associated point mutation disables the steric gate of human PrimPol.Scientific reports · 2019Article
- Structural and Kinetic Studies of the Effect of Guanine N7 Alkylation and Metal Cofactors on DNA Replication.Biochemistry · 2018Article
- Ribonucleotide discrimination by translesion synthesis DNA polymerases.Critical reviews in biochemistry and molecular biology · 2018Review
- Human DNA polymerase η accommodates RNA for strand extension.The Journal of biological chemistry · 2017Article
- The Incorporation of Ribonucleotides Induces Structural and Conformational Changes in DNA.Biophysical journal · 2017Article
- RNase HII Saves rnhA Mutant Escherichia coli from R-Loop-Associated Chromosomal Fragmentation.Journal of molecular biology · 2017Article
- The role of RNase H2 in processing ribonucleotides incorporated during DNA replication.DNA repair · 2017Article
- Ribonucleotide incorporation by human DNA polymerase η impacts translesion synthesis and RNase H2 activity.Nucleic acids research · 2017Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Ribonucleotides are frequently incorporated into DNA during replication, they are normally removed, and failure to remove them results in replication stress. This stress correlates with DNA polymerase (Pol) stalling during bypass of ribonucleotides in DNA templates. Here we demonstrate that stalling by yeast replicative Pols δ and ε increases as the number of consecutive template ribonucleotides increases from one to four. The homologous bacteriophage RB69 Pol also stalls during ribonucleotide bypass, with a pattern most similar to that of Pol ε. Crystal structures of an exonuclease-deficient variant of RB69 Pol corresponding to multiple steps in single ribonucleotide bypass reveal that increased stalling is associated with displacement of Tyr391 and an unpreferred C2'-endo conformation for the ribose. Even less efficient bypass of two consecutive ribonucleotides in DNA correlates with similar movements of Tyr391 and displacement of one of the ribonucleotides along with the primer-strand DNA backbone. These structure-function studies have implications for cellular signaling by ribonucleotides, and they may be relevant to replication stress in cells defective in ribonucleotide excision repair, including humans suffering from autoimmune disease associated with RNase H2 defects.
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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.