Reginald John Ellis FRS (born 12 February 1935) is a British scientist.
R. John Ellis | |
|---|---|
| Born | 12 February 1935 |
| Alma mater | King's College London |
| Awards | Gairdner Foundation International Award (2004) |
| Scientific career | |
| Notable students | Jane Silverthorne |
Early life and education
editEllis was educated at Highbury Grammar School, London. He studied at King's College, London and obtained a BSc degree in 1956 and PhD in 1960, for thesis research on the enzymology of transamination. He was supervised by Professor D. D. Davies.
Career
editEllis became scientific officer in the ARC (Agriculture Research Council) Unit of Plant Physiology, Imperial College, University of London, 1959–61 and an ARC Research Fellow at the Department of Biochemistry, University of Oxford, 1961–64, working on the regulation of bacterial sulphate reduction with Professor C. A. Pasternak.
In 1964, Ellis joined the University of Aberdeen as a lecturer in the Department of Botany, and moved to its Department of Biochemistry in 1968, following a visiting professorship in the University of Toronto in 1967.
In 1970, Ellis moved to the newly created Department of Biological Sciences, University of Warwick, as senior lecturer and founding head of the Chloroplast Research Group. Ellis has remained at Warwick University as reader (1973), holder of a personal chair (1976), and emeritus professor (1996). He was a visiting professor at the Department of Chemistry, University of Oxford from 1996 until 2000. From 1990 until 2009, he organised annual meetings of the UK Molecular Chaperone Club at the Universities of Oxford, Cambridge, London, Bristol, Birmingham and Warwick.
Ellis is the author of How Science Works: Evolution.[1]
Principal research achievements
edit- 1973: First identification of a product of protein synthesis by chloroplast ribosomes.[2]
- 1978: First demonstration of in vitro post-translational protein transport.[3]
- 1980: First demonstration of the binding of a chaperone to a newly synthesised polypeptide.[4]
- 1987: Formulation of the general concept of molecular chaperone function.[5]
- 1988: Discovery of the chaperonins.[6]
- 2000: First demonstration that macromolecular crowding affects protein folding and aggregation.[7]
Awards
edit- 1980: Tate & Lyle Award for contributions to plant biochemistry.
- 1983: Elected Fellow of the Royal Society of London for contributions to chloroplast biogenesis.
- 1983: Five-year Senior Research Fellowship of the Science and Engineering Research Council to work on chaperone-assisted protein assembly.
- 1986: Elected Member of EMBO, the European Molecular Biology Organisation.
- 1992: Senior Research Fellowship at St John's College, University of Oxford.
- 1997: Appointed Academic Visitor for four years at University of Oxford to work on protein folding with Professor Chris M. Dobson FRS in the Department of Chemistry.
- 2004: Gairdner Foundation International Award for "fundamental discoveries in chaperone-assisted protein folding in the cell and its relevance to neurodegeneration".[8]
- 2007: Cell Stress Society International Medal for "pioneering research on the chaperonins".
- 2011: Croonian Prize Lecture of the Royal Society for "pioneering contributions to biochemistry, molecular biology, and also plant sciences".
- 2018: The 2019 Centenary Award of the Biochemical Society.[9]
References
edit- ^ Ellis, J. (2010) How Science Works: Evolution. Springer, Heidelberg.
- ^ Blair, G. E.; Ellis, R. J. (1973). "Protein synthesis in chloroplasts. I. Light-driven synthesis of the large subunit of Fraction I protein by isolated pea chloroplasts". Biochim. Biophys. Acta. 319 (2): 223. doi:10.1016/0005-2787(73)90013-0. PMC 1178671. PMID 5076673.
- ^ Highfield, P. E.; Ellis, R. J. (1978). "Synthesis and transport of the small subunit of chloroplast ribulose bisphosphate carboxylase". Nature. 271 (5644): 420. Bibcode:1978Natur.271..420H. doi:10.1038/271420a0. S2CID 4188202.
- ^ Barraclough, R.; Ellis, R. J. (1980). "Protein synthesis in chloroplasts IX. Assembly of newly-synthesised large subunits into ribulose bisphosphate carboxylase in isolated intact pea chloroplasts". Biochim. Biophys. Acta. 608 (1): 19–31. doi:10.1016/0005-2787(80)90129-x. PMID 7388030.
- ^ Ellis, R. J. (1987). "Proteins as molecular chaperones". Nature. 328 (6129): 378–9. doi:10.1038/328378a0. PMID 3112578. S2CID 4337273.
- ^ Hemmingsen, S. M.; Woolford, C.; van der Vies, S. M.; Tilly, K.; Dennis, D. T.; Georgopoulos, C. P.; Hendrix, R. W.; Ellis, R. J. (1988). "Homologous plant and bacterial proteins chaperone oligomeric protein assembly". Nature. 333 (6171): 330–334. Bibcode:1988Natur.333..330H. doi:10.1038/333330a0. PMID 2897629. S2CID 4325057.
- ^ van den Berg, B.; Wain, R.; Dobson, C. M.; Ellis, R. J. (2000). "Macromolecular crowding perturbs protein refolding kinetics: implications for protein folding inside the cell". EMBO J. 19 (15): 3870–3875. doi:10.1093/emboj/19.15.3870. PMC 306593. PMID 10921869.
- ^ R. John Ellis Archived 28 August 2008 at the Wayback Machine, awardee of The Gairdner Foundation.
- ^ "2019 Winners". www.biochemistry.org. Archived from the original on 8 April 2018.