Characterization of three mycobacterial DinB (DNA polymerase IV) paralogs highlights DinB2 as naturally adept at ribonucleotide incorporation
Open accessAbstract
This study unveils Mycobacterium smegmatis DinB2 as the founder of a clade of Y-family DNA polymerase that is naturally adept at incorporating ribonucleotides by virtue of a leucine in lieu of a canonical aromatic steric gate. DinB2 efficiently scavenges limiting dNTP and rNTP substrates in the presence of manganese. DinB2's sugar selectivity factor, gauged by rates of manganese-dependent dNMP versus rNMP addition, is 2.7- to 3.8-fold. DinB2 embeds ribonucleotides during DNA synthesis when rCTP and dCTP are at equimolar concentration. DinB2 can incorporate at least 16 consecutive ribonucleotides. In magnesium, DinB2 has a 26- to 78-fold lower affinity for rNTPs than dNTPs, but only a 2.6- to 6-fold differential in rates of deoxy versus ribo addition (kpol). Two other M. smegmatis Y-family polymerases, DinB1 and DinB3, are characterized here as template-dependent DNA polymerases that discriminate strongly against ribonucleotides, a property that, in the case of DinB1, correlates with its aromatic steric gate side chain. We speculate that the unique ability of DinB2 to utilize rNTPs might allow for DNA repair with a 'ribo patch' when dNTPs are limiting. Phylogenetic analysis reveals DinB2-like polymerases, with leucine, isoleucine or valine steric gates, in many taxa of the phylum Actinobacteria.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Oxidatively damaged lesions may occur in RNA if rNMP incorporation numbers are high.
“Oxidatively-damaged lesions may also occur in RNA provided that rNMP incorporation numbers are high”
From Ribonucleotide errors, RNase HII, and ribonucleotide excision repair (2026) · cites this paper as Ordonez et al. 2014
The Results section, “DinB2 can embed ribonucleotides during DNA synthesis” (page unavailable), reports substantial rNMP incorporation in laboratory reactions. It does not say that oxidative lesions occur in RNA or connect their occurrence to high rNMP incorporation numbers; the measured incorporation was into DNA. (LLM, conf=0.79)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Courcelle, J., Khodursky, A., Peter, B., Brown, P. O., & Hanawalt, P. C. (2001) · Genetics · doi:10.1093/genetics/158.1.41 · Cited by 853 · see citing works
Boshoff, H. I., Reed, M. B., Barry, C. E., & Mizrahi, V. (2003) · Cell · doi:10.1016/s0092-8674(03)00270-8 · Cited by 411 · see citing works
Abundant ribonucleotide incorporation into DNA by yeast replicative polymerases
McElhinny, S. A. N., Watts, B. E., Kumar, D., Watt, D. L., Lundström, E.-B., Burgers, P., Johansson, E., Chabes, A., & Kunkel, T. A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914857107 · Cited by 409 · see citing works
SOS Mutator DNA Polymerase IV Functions in Adaptive Mutation and Not Adaptive Amplification
McKenzie, G. J., Lee, P. L., Lombardo, M.-J., Hastings, P. J., & Rosenberg, S. M. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00204-0 · Cited by 305 · see citing works
Bacterial DNA repair by non-homologous end joining
Shuman, S., & Glickman, M. S. (2007) · Nature Reviews Microbiology · doi:10.1038/nrmicro1768 · Cited by 301 · see citing works
Self-citationA single amino acid governs enhanced activity of DinB DNA polymerases on damaged templates
Jarosz, D. F., Godoy, V. G., Delaney, J. C., Essigmann, J. M., & Walker, G. C. (2006) · Nature · doi:10.1038/nature04318 · Cited by 258 · see citing works
Gong, C., Bongiorno, P., Martins, A., Stephanou, N. C., Zhu, H., Shuman, S., & Glickman, M. S. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb915 · Cited by 215 · see citing works
Self-citationUnlocking the Sugar “Steric Gate” of DNA Polymerases
Brown, J. A., & Suo, Z. (2011) · Biochemistry · doi:10.1021/bi101915z · Cited by 206 · see citing works
SOS-induced DNA polymerases enhance long-term survival and evolutionary fitness
Yeiser, B., Pepper, E. D., Goodman, M. F., & Finkel, S. E. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.092269199 · Cited by 202 · see citing works
Biochemical and Genetic Analysis of the Four DNA Ligases of Mycobacteria
Gong, C., Martins, A., Bongiorno, P., Glickman, M. S., & Shuman, S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401841200 · Cited by 137 · see citing works
Self-citationThe pathways and outcomes of mycobacterial NHEJ depend on the structure of the broken DNA endsPreprint
Aniukwu, J., Glickman, M. S., & Shuman, S. (2008) · Genes & Development · doi:10.1101/gad.1631908 · Cited by 125 · see citing works
Self-citationShee, C., Gibson, J. L., Darrow, M. C., González, C., & Rosenberg, S. M. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1104681108 · Cited by 120 · see citing works
Warner, D. F., Ndwandwe, D. E., Abrahams, G. L., Kana, B. D., Machowski, E. E., Venclovas, Č., & Mizrahi, V. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1002614107 · Cited by 120 · see citing works
Frank, E. G., & Woodgate, R. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702159200 · Cited by 115 · see citing works
Bjedov, I., Dasgupta, C. N., Slade, D., Blastier, S. L., Selva, M., & Matić, I. (2007) · Genetics · doi:10.1534/genetics.107.072405 · Cited by 91 · see citing works
AdnAB: a new DSB-resecting motor–nuclease from mycobacteriaPreprint
Sinha, K. M., Unciuleac, M.-C., Glickman, M. S., & Shuman, S. (2009) · Genes & Development · doi:10.1101/gad.1805709 · Cited by 89 · see citing works
Self-citationTompkins, J. D., Nelson, J. L., Hazel, J. C., Leugers, S. L., Stumpf, J. D., & Foster, P. L. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.11.3469-3472.2003 · Cited by 85 · see citing works
DeLucia, A. M. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg417 · Cited by 83 · see citing works
Structure of a NHEJ Polymerase-Mediated DNA Synaptic Complex
Brissett, N. C., Pitcher, R. S., Juárez, R., Picher, Á. J., Green, A., Dafforn, T. R., Fox, G. C., Blanco, L., & Doherty, A. J. (2007) · Science · doi:10.1126/science.1145112 · Cited by 83 · see citing works
A Conserved Tyr Residue Is Required for Sugar Selectivity in a Pol α DNA Polymerase
Yang, G., Franklin, M. C., Li, J., Lin, T., & Konigsberg, W. H. (2002) · Biochemistry · doi:10.1021/bi0202171 · Cited by 81 · see citing works
Sinha, K. M., Stephanou, N. C., Gao, F., Glickman, M. S., & Shuman, S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701167200 · Cited by 74 · see citing works
Self-citationAkey, D. L., Martins, A., Aniukwu, J., Glickman, M. S., Shuman, S., & Berger, J. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513550200 · Cited by 68 · see citing works
Self-citationZhu, H., Nandakumar, J., Aniukwu, J., Wang, L., Glickman, M. S., Lima, C. D., & Shuman, S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0509083103 · Cited by 63 · see citing works
Self-citationRole of the DinB Homologs Rv1537 and Rv3056 in Mycobacterium tuberculosis
Kana, B. D., Abrahams, G. L., Sung, N., Warner, D. F., Gordhan, B. G., Machowski, E. E., Tsenova, L., Sacchettini, J. C., Stoker, N. G., Kaplan, G., et al. (2010) · Journal of Bacteriology · doi:10.1128/jb.01135-09 · Cited by 60 · see citing works
Zhu, H., & Shuman, S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504002200 · Cited by 58 · see citing works
Self-citationDomain Requirements for DNA Unwinding by Mycobacterial UvrD2, an Essential DNA Helicase
Sinha, K. M., Stephanou, N. C., Unciuleac, M.-C., Glickman, M. S., & Shuman, S. (2008) · Biochemistry · doi:10.1021/bi800725q · Cited by 47 · see citing works
Self-citationStructure of a Preternary Complex Involving a Prokaryotic NHEJ DNA Polymerase
Brissett, N. C., Martín, M. J., Pitcher, R. S., Bianchi, J., Juárez, R., Green, A., Fox, G. C., Blanco, L., & Doherty, A. J. (2011) · Molecular Cell · doi:10.1016/j.molcel.2010.12.026 · Cited by 45 · see citing works
Vaisman, A., Kuban, W., McDonald, J. P., Karata, K., Yang, W., Goodman, M. F., & Woodgate, R. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks233 · Cited by 43 · see citing works
Sharma, A. S., Kottur, J., Narayanan, N., & Nair, D. T. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt146 · Cited by 42 · see citing works
Gordhan, B. G., Andersen, S. J., Meyer, A. R. D., & Mizrahi, V. (1996) · Gene · doi:10.1016/0378-1119(96)00350-2 · Cited by 42 · see citing works
Mizrahi, V., & Huberts, P. (1996) · Nucleic Acids Research · doi:10.1093/nar/24.24.4845 · Cited by 37 · see citing works
Sinha, K. M., Glickman, M. S., & Shuman, S. (2009) · Biochemistry · doi:10.1021/bi900103d · Cited by 36 · see citing works
Self-citationUnciuleac, M.-C., & Shuman, S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.076133 · Cited by 33 · see citing works
Self-citationUnciuleac, M.-C., & Shuman, S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.162925 · Cited by 33 · see citing works
Self-citationYakovleva, L., & Shuman, S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603302200 · Cited by 32 · see citing works
Self-citationYakovleva, L. M., & Shuman, S. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks417 · Cited by 27 · see citing works
Self-citationOrdonez, H., & Shuman, S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.466854 · Cited by 27 · see citing works
Self-citationKinetic Basis of Sugar Selection by a Y-Family DNA Polymerase from Sulfolobus solfataricus P2
Sherrer, S. M., Beyer, D. C., Xia, C. X., Fowler, J. D., & Suo, Z. (2010) · Biochemistry · doi:10.1021/bi101465n · Cited by 26 · see citing works
Zhu, H., Bhattarai, H. K., Yan, H.-G., Shuman, S., & Glickman, M. S. (2012) · Biochemistry · doi:10.1021/bi301202e · Cited by 24 · see citing works
Self-citationHuberts, P., & Mizrahi, V. (1995) · Gene · doi:10.1016/0378-1119(95)00453-d · Cited by 16 · see citing works
Ordonez, H., Unciuleac, M., & Shuman, S. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks046 · Cited by 13 · see citing works
Self-citation
Flagged first, then by citations
Research works printed but not linked: 2
- [21]Shuman S. Glickman M.S. Bacterial DNA repair by nonhomologous end joining Nat. Rev. Microbiol. 2007 5 852 861 17938628
- [30]Bjedov I. Dasgupta C.N. Slade D. Le Blastier S. Selva M. Matic I. Involvement of Escherichia coli DNA polymerase IV in tolerance of cytotoxic alkylating DNA lesions in vivo Genetics 2007 176 1431 4140 17483416 PMC1931539
Cited by
Sorted by citations
Gupta, R., Chatterjee, D., Glickman, M. S., & Shuman, S. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw1046 · Cited by 110 · see citing works
Self-citationGuardians of the mycobacterial genome: A review on DNA repair systems in Mycobacterium tuberculosis
Singh, A. (2017) · Microbiology · doi:10.1099/mic.0.000578 · Cited by 63 · see citing works
Pereira, W. A., Pereira, C. D. D. S., Assunção, R. G., da Silva, I. S. C., Rego, F. S., Alves, L. S. R., Santos, J., Nogueira, F. J. R., Zagmignan, A., Thomsen, T. T., et al. (2021) · Biomolecules · doi:10.3390/biom11020302 · Cited by 62 · see citing works
DNA Replication in Mycobacterium tuberculosis
Ditse, Z., Lamers, M. H., & Warner, D. F. (2017) · Microbiology Spectrum · doi:10.1128/microbiolspec.tbtb2-0027-2016 · Cited by 54 · see citing works
New insights into the structures and interactions of bacterial Y-family DNA polymerases
Timinskas, K., & Venclovas, Č. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz198 · Cited by 40 · see citing works
Structural accommodation of ribonucleotide incorporation by the DNA repair enzyme polymerase Mu
Moon, A. F., Pryor, J. M., Ramsden, D. A., Kunkel, T. A., Bębenek, K., & Pedersen, L. C. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx527 · Cited by 40 · see citing works
Ribonucleotide discrimination by translesion synthesis DNA polymerases
Vaisman, A., & Woodgate, R. (2018) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2018.1483889 · Cited by 38 · see citing works
Mutagenic cost of ribonucleotides in bacterial DNA
Schroeder, J. W., Randall, J. R., Hirst, W. G., O’Donnell, M. E., & Simmons, L. A. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1710995114 · Cited by 37 · see citing works
Ordonez, H., & Shuman, S. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku1027 · Cited by 37 · see citing works
Self-citationRibonucleotides in bacterial DNA
Schroeder, J. W., Randall, J. R., Matthews, L. A., & Simmons, L. A. (2014) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2014.981647 · Cited by 29 · see citing works
Ribonucleotide incorporation into DNA during DNA replication and its consequences
Zhou, Z.-X., Williams, J. S., Lujan, S. A., & Kunkel, T. A. (2021) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2020.1869175 · Cited by 30 · see citing works
DNA Ligase C and Prim-PolC participate in base excision repair in mycobacteria
Płociński, P., Brissett, N. C., Bianchi, J., Brzostek, A. M., Korycka‐Machała, M., Dziembowski, A., Dziadek, J., & Doherty, A. J. (2017) · Nature Communications · doi:10.1038/s41467-017-01365-y · Cited by 28 · see citing works
Substrate Specificity for Bacterial RNases HII and HIII Is Influenced by Metal Availability
Randall, J. R., Hirst, W. G., & Simmons, L. A. (2017) · Journal of Bacteriology · doi:10.1128/jb.00401-17 · Cited by 25 · see citing works
Dupuy, P., Ghosh, S., Adefisayo, O. O., Buglino, J. A., Shuman, S., & Glickman, M. S. (2022) · Nature Communications · doi:10.1038/s41467-022-32022-8 · Cited by 22 · see citing works
Self-citationLemor, M., Kong, Z., Henry, E., Brizard, R., Laurent, S., Bossé, A., & Henneke, G. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.10.004 · Cited by 18 · see citing works
Salini, S., Bhat, S. G., Naz, S., Natesh, R., Kumar, R. A., Nandicoori, V. K., & Kurthkoti, K. (2022) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01773-21 · Cited by 18 · see citing works
Ghosh, S., Samaddar, S., Kirtania, P., & GUPTA, S. K. (2015) · Journal of Bacteriology · doi:10.1128/jb.00669-15 · Cited by 17 · see citing works
A polar filter in DNA polymerases prevents ribonucleotide incorporation
Johnson, M. K., Kottur, J., & Nair, D. T. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz792 · Cited by 15 · see citing works
DNA Replication Fidelity in the Mycobacterium tuberculosis Complex
Warner, D. F., Rock, J. M., Fortune, S. M., & Mizrahi, V. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-64371-7_13 · Cited by 14 · see citing works
Ghosh, S., Goldgur, Y., & Shuman, S. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa075 · Cited by 14 · see citing works
Self-citationJacewicz, A., & Shuman, S. (2015) · Journal of Bacteriology · doi:10.1128/jb.00268-15 · Cited by 12 · see citing works
Self-citationThe Impact of RNA-DNA Hybrids on Genome Integrity in Bacteria
McLean, E. K., Nye, T. M., Lowder, F. C., & Simmons, L. A. (2022) · Annual Review of Microbiology · doi:10.1146/annurev-micro-102521-014450 · Cited by 11 · see citing works
Schmier, B. J., Chen, X., Wolin, S. L., & Shuman, S. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx038 · Cited by 11 · see citing works
Self-citationNg, W. L., & Rego, E. H. (2024) · mSphere · doi:10.1128/msphere.00122-24 · Cited by 11 · see citing works
New molecular mechanisms related to drug resistance in tuberculosis
Zenteno‐Cuevas, R. (2022) · Microbes Infection and Chemotherapy · doi:10.54034/mic.e1318 · Cited by 9 · see citing works
Roles for mycobacterial DinB2 in frameshift and substitution mutagenesis
Dupuy, P., Ghosh, S., Adefisayo, O. O., Bean, J., Gupta, R., Shuman, S., & Glickman, M. S. (2023) · eLife · doi:10.7554/elife.83094 · Cited by 8 · see citing works
Self-citationNye, T. M., McLean, E. K., Burrage, A. M., Dennison, D. D., Kearns, D. B., & Simmons, L. A. (2021) · Molecular Microbiology · doi:10.1111/mmi.14601 · Cited by 7 · see citing works
Targeting DNA Repair Systems in Antitubercular Drug Development
Minias, A. E., Brzostek, A. M., & Dziadek, J. (2018) · Current Medicinal Chemistry · doi:10.2174/0929867325666180129093546 · Cited by 8 · see citing works
Bálint, É., & Unk, I. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218248 · Cited by 7 · see citing works
Processing of matched and mismatched rNMPs in DNA by archaeal ribonucleotide excision repair
Reveil, M., Chapel, L., Vourc’h, B., Bossé, A., Vialle, L., Brizard, R., Moalic, Y., Jebbar, M., & Henneke, G. (2023) · iScience · doi:10.1016/j.isci.2023.108479 · Cited by 5 · see citing works
Patra, M. M., Ghosh, P., Sengupta, S., & GUPTA, S. K. (2021) · Microbiology · doi:10.1099/mic.0.001097 · Cited by 5 · see citing works
Ng, W. L., & Rego, E. H. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.06.12.544663 · Cited by 5 · see citing works
Diversity and distribution of bacterial DNA polymerases
Timinskas, K., Kazlauskas, D., Timinskas, A., & Venclovas, Č. (2026) · Nucleic Acids Research · doi:10.1093/nar/gkag133 · Cited by 3 · see citing works
Barman, A., Patra, M. M., & GUPTA, S. K. (2022) · Microbiology · doi:10.1099/mic.0.001192 · Cited by 3 · see citing works
Genome-wide ribonucleotide detection in <i>Archaea</i>
Moalic, Y., Reveil, M., Kundnani, D. L., Balachander, S., Yang, T., Gombolay, A., Ranjbarian, F., Brizard, R., Durand, P., Myllykallio, H., et al. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf1231 · Cited by 2 · see citing works
Pérez-Martínez, D. E., Mejía‐Ponce, P. M., Licona‐Cassani, C., de Igartua, E., Bermúdez, G., Viveros, D., & Zenteno‐Cuevas, R. (2023) · Integrated science · doi:10.1007/978-3-031-15955-8_18 · Cited by 2 · see citing works
DNA Replication in Mycobacterium tuberculosis
Ditse, Z., Lamers, M. H., & Warner, D. F. (2017) · ASM Press eBooks · doi:10.1128/9781555819569.ch27 · Cited by 2 · see citing works
Lowder, F. C., Kendal, A. H., & Simmons, L. A. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.22.696026 · Cited by 2 · see citing works
Ribonucleotide errors, RNase HII, and ribonucleotide excision repair
Cresti, J. R., & Simmons, L. A. (2026) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2026.2704628
“Both replicative and translesion DNA polymerases make sugar errors (Nick McElhinny et al. 2010; Vaisman et al. 2013; Yao et al. 2013; Ordonez et al. 2014). rNMPs, which have C3 ′ -endo sugars, cause DNA to adopt a conformation that closely resembles A-form in regions where they are embedded…”
Dupuy, P., & Glickman, M. S. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.11.09.515703
Dupuy, P., & Glickman, M. S. (2023) · Journal of Bacteriology · doi:10.1128/jb.00431-22
Mycobacterium tuberculosis as a model system
Barnard, E., Elgrail, M. M., Fay, A., Ozakman, Y., & Glickman, M. S. (2026) · Journal of Bacteriology · doi:10.1128/jb.00609-25
DNA polymerase I and DnaE mediate RNA-templated DNA synthesis over embedded ribonucleotides
Lowder, F. C., Kendal, A. H., & Simmons, L. A. (2026) · Nucleic Acids Research · doi:10.1093/nar/gkag971
- Authors
- Ordonez, H., Uson, M. L., & Shuman, S.
- Affiliations
- Memorial Sloan Kettering Cancer Center (US)
- Corresponding author
- Shuman, Stewart
- ORCID
- Shuman, Stewart
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2014-09-08
- Volume
- 42
- Issue
- 17
- Pages
- 11056-11070
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- PMC
- PMC4176160
- OpenAlex
- W2010483150
- Cited by
- 46
- References
- 41
- Citations by year
- 2026: 4 · 2025: 2 · 2024: 1 · 2023: 5 · 2022: 6 · 2021: 3 · 2020: 3 · 2019: 4 · 2018: 4 · 2017: 9 · 2016: 1 · 2015: 2 · 2014: 2
- FWCI
- 1.91
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nucleic Acids Research (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Cancer Institute (P30CA008748)
- National Institute of Allergy and Infectious Diseases (AI 64693, R01AI064693)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- DinB, Y-family DNA polymerases, Mycobacterium smegmatis, ribonucleotide incorporation, DNA repair, actinobacteria, paralogs
- MeSH terms
- Bacterial Proteins, Cations, Divalent, Deoxyribonucleotides, DNA, Manganese, Mycobacterium tuberculosis, Ribonucleotides, RNA, Templates, Genetic, DNA Primers, Amino Acid Substitution, DNA Polymerase beta, Mycobacterium smegmatis
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review