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Nigel D.F. Grindley

 

Molecular Biophysics & Biochemistry; Microbiology

Professor of Molecular Biophysics & Biochemistry

Education

B.A. Cambridge University 1967
Ph.D. London University 1974

Research Interests

A unifying theme of our research is the study of enzymes that make and break phosphodiester bonds in DNA. Our research focuses on the detailed biochemical mechanisms of (i) site-specific recombination mediated by the prototypical serine recombinase, gd resolvase, and (ii) DNA synthesis and degradation mediated by the DNA polymerases Pol I (of E. coli), a highly accurate family A polymerase, and Dbh, an inaccurate family Y polymerase, which acts specifically to bypass damaged bases in the template strand during replication. In all three cases, we have detailed structural information obtained through collaborations with the X-ray crystallography group of Tom Steitz. In addition to using standard biochemical methods, we have recently added fluorescence techniques to dissect the biochemical pathways and define the nature and the role of the conformational transitions that take place during the processes of recombination or polymerase action.

Links

• Grindley Homepage

Recent Publications

• Grindley, N.D.F., Whiteson, K.L., and Rice, P.A. (2006). Mechanisms of site-specific recombination. Ann. Rev. Biochem. 75:567-605.
• Li, W., Kamtekar, S., Xiong, Y., Sarkis, G.J., Grindley, N.D.F., and Steitz, T.A. (2005). Structure of a synaptic ƒÁƒÂ resolvase tetramer covalently linked to two cleaved DNAs. Science 309:1210-1215.

Contact

E-mail
nigel.grindley@yale.edu