ArticleOrganic & biomolecular chemistry2010
Toward a designed genetic system with biochemical function: polymerase synthesis of single and multiple size-expanded DNA base pairs.
Article in Organic & biomolecular chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Effect of Molecular Crowding on DNA Polymerase Reactions along Unnatural DNA Templates.Molecules (Basel, Switzerland) · 2020Article
- The Structural Basis for Processing of Unnatural Base Pairs by DNA Polymerases.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020Review
- DNA polymerase θ specializes in incorporating synthetic expanded-size (xDNA) nucleotides.Nucleic acids research · 2016Article
- Computational Evaluation of Nucleotide Insertion Opposite Expanded and Widened DNA by the Translesion Synthesis Polymerase Dpo4.Molecules (Basel, Switzerland) · 2016Article
- Artificial genetic sets composed of size-expanded base pairs.Angewandte Chemie (International ed. in English) · 2013Review
- Fluorescent DNA-based enzyme sensors.Chemical Society reviews · 2011Review
- Encoding phenotype in bacteria with an alternative genetic set.Journal of the American Chemical Society · 2011Article
- Reversible bond formation enables the replication and amplification of a crosslinking salen complex as an orthogonal base pair.Nature chemistry · 2011Article
- Chemistry of nucleic acids: impacts in multiple fields.Chemical communications (Cambridge, England) · 2011Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
The development of alternative architectures for genetic information-encoding systems offers the possibility of new biotechnological tools as well as basic insights into the function of the natural system. In order to examine the potential of benzo-expanded DNA (xDNA) to encode and transfer biochemical information, we carried out a study of the processing of single xDNA pairs by DNA Polymerase I Klenow fragment (Kf, an A-family sterically rigid enzyme) and by the Sulfolobus solfataricus polymerase Dpo4 (a flexible Y-family polymerase). Steady-state kinetics were measured and compared for enzymatic synthesis of the four correct xDNA pairs and twelve mismatched pairs, by incorporation of dNTPs opposite single xDNA bases. Results showed that, like Kf, Dpo4 in most cases selected the correctly paired partner for each xDNA base, but with efficiency lowered by the enlarged pair size. We also evaluated kinetics for extension by these polymerases beyond xDNA pairs and mismatches, and for exonuclease editing by the Klenow exo+ polymerase. Interestingly, the two enzymes were markedly different: Dpo4 extended pairs with relatively high efficiencies (within 18-200-fold of natural DNA), whereas Kf essentially failed at extension. The favorable extension by Dpo4 was tested further by stepwise synthesis of up to four successive xDNA pairs on an xDNA template.
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Registered trials
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