• Tony Maxwell's Research

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Curriculum Vitae

• 1977 B.Sc: Biochemistry, University College London
• 1981 Ph.D: Biochemistry, University of Bristol
• 1982-1986 Postdoc: NIH, Bethesda, MD, USA
• 1994-1997 Lecturer: Dept. Biochemistry University of Leicester
• 1994-1997 Reader: Dept. Biochemistry University of Leicester
• 1991-1997 Lister-Jenner Research Fellow: Dept. Biochemistry University of Leicester
• 1997-2000 Professor: Dept. Biochemistry University of Leicester
• 2000-present Head of Department: Dept. Biological Chemistry, John Innes Centre
• 2001-present Honorary Chair: University of East Anglia

Tony Maxwell

Head of Department

Biological Chemistry

Contact details

Tel: +44 (0)1603 450771
tony.maxwell@jic.ac.uk

Research interests

DNA topoisomerases in bacteria and plants: mechanism and drug-targeting

Overall aims and objectives: to investigate the structure and mechanism of DNA topoisomerases and associated proteins, in order to further our understanding of key biological processes in which they are involved, and to harness this knowledge for the development of therapeutic agents.

DNA topoisomerases are a vitally important class of proteins involved in the control of the topological state of DNA. Their major biological functions are in DNA replication, transcription and the control of gene expression. One of the best characterised DNA topoisomerases is DNA gyrase from Escherichia coli. Like all topoisomerases gyrase can relax supercoiled DNA, but it is the only enzyme of the group that can also supercoil DNA; DNA supercoiling is driven by ATP hydrolysis. In addition to studying gyrase, this laboratory is also working on a number of related enzymes. These include, topoisomerase IV from E. coli, and the recently discovered DNA gyrase and DNA topoisomerase VI from Arabidopsis thaliana.

Topoisomerases provide fascinating systems for the study of DNA-protein interactions and energy coupling in biological systems. Their study also has clinical relevance from the standpoint of antibacterial and anti-tumour drugs. For example, gyrase is the target for two clinically important classes of antibiotics, the quinolones and the coumarins, which have been found to inhibit different stages of the supercoiling reaction. It is also the target of a number of bacterial toxins (e.g CcdB and microcin). The major interests in this laboratory are enzyme structure and mechanism, and the interaction of the enzymes with drugs. For example, we have crystallised active fragments of the E. coli gyrase A and B proteins and the structure of some of these have been solved to high resolution by x-ray crystallography. We are also investigating the physiological role of gyrase and topo VI in Arabidopsis thaliana. This information is yielding valuable insight into mechanistic and drug-targeting aspects of gyrase and other topoisomerases. This work involves a wide range of methodologies including bacteriology, mutagenesis, protein engineering, plant molecular biology, enzymology and biophysical methods.