Professor Dale Wigley and his team in the Section of Structural Biology are working on what happens when the DNA in a cell is damaged, and in particular how DNA breaks are repaired. If such DNA damage is not repaired correctly, mistakes occur in important genes which can lead to cancer.
Professor Wigley studies bacteria to investigate how they repair DNA double-strand breaks. DNA breaks are created by some antibacterial compounds so understanding their repair will help us to understand some aspects of antibiotic resistance. In addition, bacteria are a simple model system and easier to work with than human cells. Understanding the DNA repair processes in bacteria will help Professor Wigley and his team gain insight into the similar, more complex, processes at work in human cells, the failure of which can lead to cancer.
A second area relates to understanding how the DNA in human cells is packaged and processed. The DNA is contained in the nucleus and is wrapped into structures called nucleosomes. Nucleosomes give stability to the DNA but need to be manipulated in a variety of ways to allow access to genes for transcription or to the DNA for repair. Large multi-protein complexes manipulate and regulate access to nucleosomes and Professor Wigley’s group are investigating several from the INO80 family of chromatin manipulating enzymes.
Please go to the Structural Biology Section website for news, up-to-date research summaries, a list of job opportunities, and information on lab members.
- 1985 - BSc (Hons) Biochemistry, University of York
- 1988 - PhD Biochemistry, University of Bristol
- 1988-1990,Lecturer, University of Leicester
- 1990-1992, SERC Advanced Fellow, University of York
- 1993-1997, Lecturer, University of Oxford
- 1997-2000, Reader, University of Oxford
- 2000 - 2010, Principal Scientist, Cancer Research UK
- 2010 - 2014, Professor and Head of Division, Institute Cancer Research
- 2014 - present, Professor, Department of Medicine, Imperial College London
Wigley D, Structure of the DNA-bound spacer capture complex of a Type II CRISPR-Cas system., Molecular Cell, ISSN:1097-2765
et al., 2019, CtIP forms a tetrameric dumbbell-shaped particle which bridges complex DNA end structures for double-strand break repair, Elife, Vol:8, ISSN:2050-084X
Cheng K, Wigley DB, 2018, DNA translocation mechanism of an XPD family helicase, Elife, Vol:7, ISSN:2050-084X
et al., 2018, Structure and dynamics of the yeast SWR1-nucleosome complex, Science, Vol:362, ISSN:0036-8075, Pages:199-+
et al., 2018, Structure and regulation of the human INO80-nucleosome complex, Nature, Vol:556, ISSN:0028-0836, Pages:391-+