R. John Ellis
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 |
Reginald John EllisFRS(born 12 February 1935) is a British scientist.
Early life and education[edit]
Ellis was educated atHighbury Grammar School,London. He studied atKing's College, Londonand obtained a BSc degree in 1956 and PhD in 1960, for thesis research on the enzymology oftransamination.He was supervised by Professor D. D. Davies.
Career[edit]
Ellis 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 theUniversity of Aberdeenas a lecturer in the Department of Botany, and moved to its Department of Biochemistry in 1968, following a visiting professorship in theUniversity of Torontoin 1967.
In 1970, Ellis moved to the newly created Department of Biological Sciences,University of Warwick,as senior lecturer and founding head of theChloroplastResearch 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 Oxfordfrom 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 ofHow Science Works: Evolution.[1]
Principal research achievements[edit]
- 1973: First identification of a product ofprotein synthesisby chloroplastribosomes.[2]
- 1978: First demonstration of in vitro post-translational protein transport.[3]
- 1980: First demonstration of the binding of achaperoneto a newly synthesisedpolypeptide.[4]
- 1987: Formulation of the general concept ofmolecular chaperonefunction.[5]
- 1988: Discovery of thechaperonins.[6]
- 2000: First demonstration thatmacromolecular crowdingaffectsprotein foldingand aggregation.[7]
Awards[edit]
- 1980:Tate & LyleAward for contributions to plant biochemistry.
- 1983: ElectedFellow of the Royal Societyof London for contributions to chloroplastbiogenesis.
- 1983: Five-year Senior Research Fellowship of theScience and Engineering Research Councilto work on chaperone-assisted protein assembly.
- 1986: Elected Member of EMBO, theEuropean Molecular Biology Organisation.
- 1992: Senior Research Fellowship atSt John's College,University of Oxford.
- 1997: Appointed Academic Visitor for four years atUniversity of Oxfordto work on protein folding with Professor Chris M. Dobson FRS in the Department of Chemistry.
- 2004:Gairdner Foundation International Awardfor "fundamental discoveries in chaperone-assisted protein folding in the cell and its relevance toneurodegeneration".[8]
- 2007: Cell Stress Society International Medal for "pioneering research on thechaperonins".
- 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 theBiochemical 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.PMC1178671.PMID5076673.
- ^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.S2CID4188202.
- ^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.PMID7388030.
- ^Ellis, R. J. (1987). "Proteins asmolecular chaperones".Nature.328(6129): 378–9.doi:10.1038/328378a0.PMID3112578.S2CID4337273.
- ^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.PMID2897629.S2CID4325057.
- ^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.PMC306593.PMID10921869.
- ^R. John EllisArchived28 August 2008 at theWayback Machine,awardee of The Gairdner Foundation.
- ^"2019 Winners".biochemistry.org.Archived fromthe originalon 8 April 2018.
External links[edit]
- Web pageat School of Life Sciences, University of Warwick.
- R. John Ellis.How Science Works: EvolutionEssay.
- Lectures on how science works in the context of evolution1,2,3and4.
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