ArticleNucleic acids research2009
Conferring a template-dependent polymerase activity to terminal deoxynucleotidyltransferase by mutations in the Loop1 region.
Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Substrate energetics in non-templated DNA synthesis by terminal deoxynucleotidyl transferase.Nucleic acids research · 2026Article
- Optimization of Expression and Thermostability of Terminal Deoxynucleotidyl Transferase Through Iterative Mutagenesis and Computational Design.Applied biochemistry and biotechnology · 2026Article
- Aspergillus fumigatus PolX1 is an early ancestor of vertebrate terminal deoxynucleotidyl transferases.Nucleic acids research · 2026Article
- The Role of Active Site Hydrophobic Interactions in Facilitating Catalysis in Human Terminal Deoxynucleotidyl Transferase.International journal of molecular sciences · 2025Article
- Fidelity, specialization, and evolution of Paramecium PolX DNA polymerases involved in programmed double-strand break DNA repair.Nucleic acids research · 2025Article
- Terminal deoxynucleotidyl transferase: Properties and applications.Engineering microbiology · 2025Review
- Computational Modeling Study of the Molecular Basis of dNTP Selectivity in Human Terminal Deoxynucleotidyltransferase.Biomolecules · 2024Article
- DNA polymerase λ Loop1 variant yields unexpected gain-of-function capabilities in nonhomologous end-joining.DNA repair · 2024Article
- Substrate Specificity Diversity of Human Terminal Deoxynucleotidyltransferase May Be a Naturally Programmed Feature Facilitating Its Biological Function.International journal of molecular sciences · 2024Article
- Insight into the mechanism of DNA synthesis by human terminal deoxynucleotidyltransferase.Life science alliance · 2022Article
- Article
- Structural evidence for an inThe Journal of biological chemistry · 2019Article
- A fidelity mechanism in DNA polymerase lambda promotes error-free bypass of 8-oxo-dG.The EMBO journal · 2016Article
- Article
- Functional analyses of polymorphic variants of human terminal deoxynucleotidyl transferase.Genes and immunity · 2015Article
- Essential role for polymerase specialization in cellular nonhomologous end joining.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Structural basis for a novel mechanism of DNA bridging and alignment in eukaryotic DSB DNA repair.The EMBO journal · 2015Article
- Decision-making during NHEJ: a network of interactions in human Polμ implicated in substrate recognition and end-bridging.Nucleic acids research · 2014Article
- Structures of the Leishmania infantum polymerase beta.DNA repair · 2014Article
- Nonhomologous end joining: a good solution for bad ends.DNA repair · 2014Review
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Terminal deoxynucleotidyltransferase (Tdt) and DNA polymerase mu (pol mu) are two eukaryotic highly similar proteins involved in DNA processing and repair. Despite their high sequence identity, they differ widely in their activity: pol mu has a templated polymerase activity, whereas Tdt has a non-templated one. Loop1, first described when the Tdt structure was solved, has been invoked as the major structural determinant of this difference. Here we describe attempts to transform Tdt into pol mu with the minimal number of mutations in and around Loop1. First we describe the effect of mutations on six different positions chosen to destabilize Tdt Loop1 structure, either by alanine substitution or by deletion; they result at most in a reduction of Tdt activity, but adding Co(++) restores most of this Tdt activity. However, a deletion of the entire Loop1 as in pol lambda does confer a limited template-dependent polymerase behavior to Tdt while a chimera bearing an extended pol mu Loop1 reproduces pol mu behavior. Finally, 16 additional substitutions are reported, targeted at the two so-called 'sequence determinant' regions located just after Loop1 or underneath. Among them, the single-point mutant F401A displays a sequence-specific replicative polymerase phenotype that is stable upon Co(++) addition. These results are discussed in light of the available crystal structures.
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