.PLENARY LECTURES

R. John Ellis

Ellis
My new email address is R.J.Ellis@warwick.ac.uk
www.gairdner.org/winners2004.html

CV
Dr. Ellis earned his doctorate in 1960 from King's College, London for research on transamination reactions with Professor Davies. His postdoctoral studies were done at Oxford in the Biochemistry Department on sulfate reduction in bacteria with Professor Pasternak. In 1964 Dr. Ellis joined the Departments of Botany and Biochemistry at the University of Aberdeen. He moved to the newly founded Department of Biological Sciences at the University of Warwick in 1970 as Senior Lecturer and Head of the Chloroplast Research Group. In 1976 was awarded a Personal Chair in the department and in 1983 was elected to the Royal Society for his work on chloroplast biogenesis. In 1980 he discovered the first example of a newly synthesized polypeptide that binds to another protein before it folds and assembles; this binding keeps this polypeptide, the large subunit of rubisco, from aggregating with itself. This finding led to the formulation in 1987 of the molecular chaperone concept as a new general cellular function, the term`molecular chaperone` having being proposed by Ron Laskey in 1978 to describe the properties of a nuclear protein involved in the assembly of nucleosomes. The cloning and sequencing of the rubisco binding protein led to the discovery of the chaperonin family of chaperones in 1988. Ellis continues to contribute to the development of ideas about the chaperone function.

Selected Publications
  1. Ellis, R.J. Molecular chaperones: assisting assembly as well as folding,
    Trends Biochem. Sci. 2006 7, 395-401.
  2. Ellis, R.J and Minton, A.P. Protein aggregation in crowded environments, Biological Chemistry 2006 387, 485-497.
  3. Ellis, R.J., From chloroplasts to chaperones; how one thing led to another, Photosyn. Res. 80, 333-343, 2004.
  4. Ellis RJ. Protein folding: importance of the Anfinsen cage. Curr. Biol. 2003 13, R881-R883.
  5. Ellis RJ. Macromolecular crowding: obvious but underappreciated.
  6. Trends Biochem. Sci. 2001 26, 597-604.
  7. Ellis RJ. Discovery of molecular chaperones. Cell Stress Chaperones. 1996 1, 155-160.
  8. Ellis RJ, van der Vies SM. Molecular chaperones. Annu. Rev. Biochem. 1991 60, 321-347
  9. Ellis RJ, Hemmingsen SM. Molecular chaperones: proteins essential for the biogenesis of some macromolecular structures. Trends Biochem. Sci. 1989 14, 339-342.
  10. Ellis RJ, van der Vies SM, Hemmingsen SM. The molecular chaperone concept. Biochem. Soc. Symp. 1989 55, 145-153.
  11. Hemmingsen SM, Woolford C, van der Vies SM, Tilly K, Dennis DT, Georgopoulos CP, Hendrix RW, Ellis RJ. Homologous plant and bacterial proteins chaperone oligomeric protein assembly. Nature 1988, 333, 330-334.
  12. Ellis, R.J., Proteins as molecular chaperones, Nature 328, 378-379, 1987.
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