Imperial College London

Professor Dale Wigley FRS

Faculty of MedicineDepartment of Medicine

Chair in Protein Crystallography



+44 (0)20 7594 8417d.wigley




Mrs Kasia Pearce +44 (0)20 7594 2763




258Sir Alexander Fleming BuildingSouth Kensington Campus





mini cv

  • 1985 - BSc (Hons) Biochemistry, University of York                                  
  • 1988 - PhD Biochemistry, University of Bristol                                              
  • 1988-1990,Temporary 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, Section of Structural Biology, Department of Medicine, Imperial College London                           






 Professor Dale Wigley and his team at the Imperial College London are finding out what happens when the DNA in a cell is damaged, and how the cell deals with it. If DNA damage is not repaired correctly, mistakes occur in important genes which can lead to cancer.

Professor Wigley studies bacteria grown in the lab to investigate DNA repair. 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.

Learning more about how cells repair damage to their DNA could lead to new ways to prevent or treat cancer in the future.

Selected recent publications 

 Krajewski, W.W., Fu, X., Wilkinson, M., Cronin, N.B., Dillingham, M.S. and Wigley, D.B. (2014), Structural basis for translocation by AddAB helicase/nuclease and its arrest at Chi sites. Nature 508, 416-9.

Wigley, D.B. (2013), Bacterial DNA repair: recent insights into the mechanism of RecBCD, AddAB and AdnAB. Nat. Rev. Microbiol. 11, 9-13.

Saikrishnan, K., Yeeles, J.T., Gilhooly, N., Krajewski, W, Dillingham, M.S. and Wigley, D.B. (2012), Insights into Chi recognition from the structure of an AddAB-typehelicase-nuclease complex. EMBO J. 31, 1568-78.

Handa, N., Yang, L., Dillingham, M.S., Kobayashi, I., Wigley, D.B. and Kowalczykowski, S.C. (2012), Molecular determinants responsible for recognition of the single-stranded DNA regulatory sequence, chi, by RecBCD enzyme. Proc. Natl. Acad. Sci. U.S.A. 109, 8901-8906.

Yang, L., Handa, N., Liu, B., Dillingham, M.S., Wigley, D.B. and Kowalczykowski, S.C. (2012), Mutation of chi-recognition by RecBCD reveals a regulated molecular latch and suggests a channel- bypass mechanism for biological control. Proc. Natl. Acad. Sci. U.S.A. 109, 8907-8912.

Saravanan, M., Wuerges, J., Bose, D., McCormack, E.A., Cook, N.J., Zhang, X. and Wigley, D.B. (2012), Interactions between the nucleosome histone core and Arp8 in the INO80 Chromatin Remodelling Complex Proc. Natl. Acad. Sci. U.S.A. 109, 20883-20888.

Saravanan M, Wuerges J, Bose D, McCormack EA, Cook NJ, Zhang X and Wigley DB (2012), Interactions between the nucleosome histone core and Arp8 in the INO80 Chromatin Remodelling Complex. Proc Natl Acad Sci USA, 109:20883-8

Saikrishnan, K., Powell, B., Cook, N., Webb, M.R. and Wigley, D.B. (2009), Mechanistic basis of 5’-3’ translocation in SF1B helicase Cell 137, 849-859.

Zhang, X. and Wigley, D.B. (2008), The ‘glutamate switch’ provides a link between ATPase activity and ligand binding in AAA+ proteins. Nat. Struct. Mol. Biol. 15, 1223-1227.

Saikrishnan, K., Griffiths, S.P., Cook, N., Court, R. and Wigley, D.B. (2008), DNA binding to RecD : role of the 1B domain in SF1B helicase activity. EMBO J. 27, 2222-2229.

Gaudier, M., Schuwirth, B.S., Westcott, S.L. and Wigley, D.B. (2007), Structural basis of DNA replication origin recognition by an ORC protein. Science 317, 1213-1216.

Singleton, M.R., Dillingham, M.S. and Wigley D.B. (2007), Structure and mechanism of helicases and nucleic acid translocases. Ann. Rev. Biochem. 76, 23-50.

Seybert, A., Singleton, M.R., Cook, N., Hall, D.R. and Wigley, D.B. (2006), Communication between subunits within an archaeal clamp loader complex. EMBO J. 25, 2209-2218




Ayala R, Willhoft O, Aramayo RJ, et al., 2018, Structure and regulation of the human INO80-nucleosome complex, Nature, Vol:556, ISSN:0028-0836, Pages:391-+

Aramayo RJ, Willhoft O, Ayala R, et al., 2018, Cryo-EM structures of the human INO80 chromatin-remodeling complex, Nature Structural & Molecular Biology, Vol:25, ISSN:1545-9993, Pages:37-+

Lin C-L, Chaban Y, Rees DM, et al., 2017, Functional characterization and architecture of recombinant yeast SWR1 histone exchange complex, Nucleic Acids Research, Vol:45, ISSN:0305-1048, Pages:7249-7260

Willhoft O, McCormack EA, Aramayo RJ, et al., 2017, Crosstalk within a functional INO80 complex dimer regulates nucleosome sliding, Elife, Vol:6, ISSN:2050-084X

Sanders K, Lin C-L, Smith AJ, et al., 2017, The structure and function of an RNA polymerase interaction domain in the PcrA/UvrD helicase, Nucleic Acids Research, Vol:45, ISSN:0305-1048, Pages:3875-3887

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