2010
Distinct Roles of the Active-site Mg2+ Ligands, Asp882 and Asp705, of DNA Polymerase I (Klenow Fragment) during the Prechemistry Conformational Transitions*
Bermek O, Grindley ND, Joyce CM. Distinct Roles of the Active-site Mg2+ Ligands, Asp882 and Asp705, of DNA Polymerase I (Klenow Fragment) during the Prechemistry Conformational Transitions*. Journal Of Biological Chemistry 2010, 286: 3755-3766. PMID: 21084297, PMCID: PMC3030377, DOI: 10.1074/jbc.m110.167593.Peer-Reviewed Original Research
2005
DNA Polymerase Catalysis in the Absence of Watson−Crick Hydrogen Bonds: Analysis by Single-Turnover Kinetics †
Potapova O, Chan C, DeLucia A, Helquist S, Kool E, Grindley N, Joyce C. DNA Polymerase Catalysis in the Absence of Watson−Crick Hydrogen Bonds: Analysis by Single-Turnover Kinetics †. Biochemistry 2005, 45: 890-898. PMID: 16411765, PMCID: PMC2567902, DOI: 10.1021/bi051792i.Peer-Reviewed Original Research
1998
Tn552 transposase catalyzes concerted strand transfer in vitro
Leschziner A, Griffin T, Grindley N. Tn552 transposase catalyzes concerted strand transfer in vitro. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 7345-7350. PMID: 9636151, PMCID: PMC22612, DOI: 10.1073/pnas.95.13.7345.Peer-Reviewed Original ResearchHow E. coli DNA polymerase I (klenow fragment) distinguishes between deoxy- and dideoxynucleotides11Edited by A. R Fersht
Astatke M, Grindley N, Joyce C. How E. coli DNA polymerase I (klenow fragment) distinguishes between deoxy- and dideoxynucleotides11Edited by A. R Fersht. Journal Of Molecular Biology 1998, 278: 147-165. PMID: 9571040, DOI: 10.1006/jmbi.1998.1672.Peer-Reviewed Original ResearchConceptsMutant derivativesWild-type Klenow fragmentKlenow fragmentTernary complexAmino acid residuesE. coli DNA polymerase IIncorporation of dNTPsDNA polymerase IDNTP ternary complexPolymerase IAcid residuesPhosphoryl transferState kinetic parametersConformational changesNatural substratePositions 762DNA polymeraseEnzyme DNAKlenow fragment DNA polymeraseDNTPsIncoming dNTPDNTPSide chain resultsRibose moietyDideoxynucleotides
1993
Analysis of a Nucleoprotein Complex: the Synaptosome of γδ Resolvase
Grindley N. Analysis of a Nucleoprotein Complex: the Synaptosome of γδ Resolvase. Science 1993, 262: 738-740. PMID: 8235593, DOI: 10.1126/science.8235593.Peer-Reviewed Original ResearchMapping interactions between the catalytic domain of resolvase and its DNA substrate using cysteine-coupled EDTA-iron.
Mazzarelli J, Ermácora M, Fox R, Grindley N. Mapping interactions between the catalytic domain of resolvase and its DNA substrate using cysteine-coupled EDTA-iron. Biochemistry 1993, 32: 2979-86. PMID: 8384484, DOI: 10.1021/bi00063a008.Peer-Reviewed Original Research
1992
Side chains involved in catalysis of the polymerase reaction of DNA polymerase I from Escherichia coli.
Polesky A, Dahlberg M, Benkovic S, Grindley N, Joyce C. Side chains involved in catalysis of the polymerase reaction of DNA polymerase I from Escherichia coli. Journal Of Biological Chemistry 1992, 267: 8417-8428. PMID: 1569092, DOI: 10.1016/s0021-9258(18)42461-1.Peer-Reviewed Original Research
1991
Resolvase‐catalysed reactions between res sites differing in the central dinucleotide of subsite I.
Stark W, Grindley N, Hatfull G, Boocock M. Resolvase‐catalysed reactions between res sites differing in the central dinucleotide of subsite I. The EMBO Journal 1991, 10: 3541-3548. PMID: 1655422, PMCID: PMC453083, DOI: 10.1002/j.1460-2075.1991.tb04918.x.Peer-Reviewed Original Research