ArticleNucleic acids research2011
Engineered split in Pfu DNA polymerase fingers domain improves incorporation of nucleotide gamma-phosphate derivative.
Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Enhanced Biomass Production of Recombinant Pfu DNA Polymerase Producer Escherichia coli BL21(DE3) by Optimization of Induction Variables Using Response Surface Methodology.The protein journal · 2023Article
- Bioorthogonal information storage in L-DNA with a high-fidelity mirror-image Pfu DNA polymerase.Nature biotechnology · 2021Article
- Engineering human PrimPol into an efficient RNA-dependent-DNA primase/polymerase.Nucleic acids research · 2017Article
- Exploring the Chemistry of Genetic Information Storage and Propagation through Polymerase Engineering.Accounts of chemical research · 2017Review
- The Toolbox for Modified Aptamers.Molecular biotechnology · 2016Review
- Modified Nucleoside Triphosphates for In-vitro Selection Techniques.Frontiers in chemistry · 2016Review
- Directed polymerase evolution.FEBS letters · 2014Review
Corrections and comments
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Authors and funding
5 authors.
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Abstract
Using compartmentalized self-replication (CSR), we evolved a version of Pyrococcus furiosus (Pfu) DNA polymerase that tolerates modification of the γ-phosphate of an incoming nucleotide. A Q484R mutation in α-helix P of the fingers domain, coupled with an unintended translational termination-reinitiation (split) near the finger tip, dramatically improve incorporation of a bulky γ-phosphate-O-linker-dabcyl substituent. Whether synthesized by coupled translation from a bicistronic (-1 frameshift) clone, or reconstituted from separately expressed and purified fragments, split Pfu mutant behaves identically to wild-type DNA polymerase with respect to chromatographic behavior, steady-state kinetic parameters (for dCTP), and PCR performance. Although naturally-occurring splits have been identified previously in the finger tip region of T4 gp43 variants, this is the first time a split (in combination with a point mutation) has been shown to broaden substrate utilization. Moreover, this latest example of a split hyperthermophilic archaeal DNA polymerase further illustrates the modular nature of the Family B DNA polymerase structure.
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