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Paul S. Freemont

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Paul Freemont is Professor of Structural and Synthetic Biology[1] in the Department of Infectious Diseases, Imperial College London.

Paul S. Freemont
Alma materHeriot-Watt University, Edinburgh, University of Aberdeen
Scientific career
FieldsSynthetic Biology, Structural Biology, X-ray crystallography, CryoEM, Cell Biology, Spectroscopy, Biophysics
InstitutionsUniversity of Aberdeen, Dept of Molecular Biophysics and Biochemistry, Yale University, ICRF, Structural and Synthetic Biology Division, Imperial College London
Doctoral advisorLinda Fothergill-Gilmore
Other academic advisorsJohn E. Fothergill,Thomas Steitz
Websitehttps://www.structurebiomed.org/paul-freemont

Career

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Paul Freemont received a bachelor's degree in Biochemistry from the Heriot-Watt University, Edinburgh,[2] and a Ph.D. in Biochemistry, Biophysics and Molecular Biology at the University of Aberdeen.[3] He was a Postdoctoral Research Associate with Thomas A. Steitz at the Dept of Molecular Biophysics and Biochemistry, Yale University.[4] In 1988 he joined the ICRF (Imperial Cancer Research Fund, Lincoln Inn Fields, now called CRUK upon the merging of CRC (Cancer Research Campaign) and ICRF and now situated at the Francis Crick Institute) as a Principal Scientist in 1987.[5] In 2001 he was appointed to a Professorship of Structural Biology in the Department of Infectious Disease at Imperial College, London.[6]

Research

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During his PhD research in the laboratory of Dr. Linda Fothergill[7] at the Dept. of Biochemistry, University of Aberdeen[8] he sequenced the proteins for two key metabolic proteins, Human skeletal-muscle fructose-bisphosphate aldolase,[9][10] and chicken skeletal-muscle enolase.[11] In 1984 Paul Freemont started a Postdoctoral Research Associate position in the laboratory of Prof. Thomas Steitz and worked on the X-ray crystallographic structure of DNA polymerase I (Klenow Fragment) and its DNA complexes in collaboration with Dr. Cathy Joyce, Prof. Thomas Steitz and group members[12][13][14] in Prof. Nigel Grindley's group in the part of Dept. of Molecular Biophysics and Biochemistry based in Yale Medical School, prior its move to the Bass Building on Science Hill. In this DNA polymerase I (Klenow fragment) research effort he was joined by Dr. Jonathan Friedman, Dr. Lorena Beese and Dr. Mark Sanderson. In collaboration with Nigel Grindley, Graham Hatfull and Mark Sanderson he worked on the X-ray crystallographic structure of the site-specific recombination enzyme γδ-resolvase.[15] Upon returning to Britain in 1987 he was appointed to a Principal Investigator position at the ICRF (Imperial Cancer Research Fund Laboratories, Lincoln Inn Fields). Here he studied a very wide spectrum of different proteins/protein complexes and enzymological problems ranging from DNA repair proteins like AP endonuclease[16] to XRCC1 BRCT[17] in collaboration with Tomas Lindahl's group, PML (promyelocytic leukemia protein) structure function studies[18][19] and the characterisation of the Ring-finger.[20][21]

After moving to Imperial College in 2001 Paul Freemont engaged in the research of a wide range of enzymological problems, among many others the structure and function studies of the p97 ATPase and also p47, the DNA repair systems in Neisseria such as the AP endonuclease in collaboration with Geoff Baldwin's group at Imperial College and more recently many papers in Synthetic Biology.[22]

Books

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Synthetic Biology - A Primer (Revised Edition) Paperback – 24 Aug. 2015 Edited by Geoff Baldwin, Travis Bayer, Robert Dickinson, Tom Ellis, Paul S Freemont, Richard I Kitney, Karen Polizzi, Guy-Bart Stan.

Awards

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Paul Freemont is a Fellow of the Royal Society of Biology

EMBO Member

Other activities and appointments

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Professor Paul Freemont is Head of the section of Structural and Synthetic Biology in the Department of Infectious Disease. Co-director of the National UK Innovation and Knowledge Centre for Synthetic Biology (SynbiCIT)[23] at Imperial College London.

References

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  1. ^ "Paul Freemont". Structural & Synthetic Biology Imperial College. Retrieved 2023-02-15.
  2. ^ "Biological Chemistry, Heriot Watt University". Biological Chemistry. Retrieved 2023-06-25.
  3. ^ "Biological Sciences". Biological Sciences, Aberdeen University.
  4. ^ "Molecular Biophysics and Biochemistry". mbb.yale.edu. Retrieved 2023-02-15.
  5. ^ "Cancer Research Network at the Crick". Cancer Research Network at the Crick. 9 July 2024.
  6. ^ "Paul Freemont". Structural & Synthetic Biology Imperial College. Retrieved 2023-02-15.
  7. ^ "Staff profiles". The University of Edinburgh. 22 September 2022. Retrieved 2023-02-15.
  8. ^ "Research | The School of Biological Sciences | The University of Aberdeen". www.abdn.ac.uk. Retrieved 2023-02-15.
  9. ^ Freemont, P.S., Dunbar, B. and Fothergill, L.A. (1984) Human skeletal-muscle aldolase: N-terminal sequence analysis of CNBr- and o-iodosobenzoic acid-cleavage fragments. Arch Biochem Biophys 228(1), 342-52.
  10. ^ Freemont, P.S., Dunbar, B., Fothergill-Gilmore, L.A. (1988) The complete amino acid sequence of human skeletal-muscle fructose-bisphosphate aldolase. Biochem J. 249(3),779-88.
  11. ^ Russell, G.A., Dunbar, B., Fothergill-Gilmore, L.A. (1986) The complete amino acid sequence of chicken skeletal-muscle enolase. Biochem J. 236(1),115-126
  12. ^ Derbyshire, V., Freemont, P.S., Sanderson, M.R., Beese, L., Friedman, J.M., Joyce, C.M. and Steitz, T.A. Genetic and crystallographic studies of the 3',5'-exonucleolytic site of DNA polymerase I. Science 240(4849),199-201 (1988)
  13. ^ Freemont, P.S., Friedman, J.M., Beese, L..S., Sanderson, M.R and  Steitz TA. Cocrystal structure of an editing complex of Klenow fragment with DNA.Proc Natl Acad Sci U S A. 85(23),8924-8 (1988).
  14. ^ Steitz, T.A., Beese, L., Freemont, P.S., Friedman, J.M. and  Sanderson, M.R. Structural studies of Klenow fragment: an enzyme with two active sites.Cold Spring Harb Symp Quant Biol. 52, 465-71 (1987)
  15. ^ "Nigel Grindley's research". Nigel Grindley's Research, Dept of Molecular Biophysics and Biochemistry, Yale. Retrieved 2023-06-25.
  16. ^ Gorman, M.A., Morera, S., Rothwell D.G., de La Fortelle, E., Mol. C.D., Tainer, J.A., Hickson, I.D. and Freemont PS.  The crystal structure of the human DNA repair endonuclease HAP1 suggests the recognition of extra-helical deoxyribose at DNA abasic sites. EMBO J. 16(21), 6548-58 (1997).
  17. ^ Zhang, X., Moréra, S., Bates, P.A., Whitehead, P.C., Coffer, A.I., Hainbucher, K., Nash, R.A., Sternberg, M.J., Lindahl, T. and Freemont, P.S. Structure of an XRCC1 BRCT domain: a new protein-protein interaction module. EMBO J. 17(21), 6404-11 (1998)
  18. ^ Hodges, M., Tissot, C., Howe, K., Grimwade, D and Freemont, P.S. Structure, organization, and dynamics of promyelocytic leukemia protein nuclear bodies. Am J Hum Genet. 63(2),297-304 (1998).
  19. ^ Cao, T., Duprez, E., Borden, K.L., Freemont, P.S. and Etkin, L.D.Ret finger protein is a normal component of PML nuclear bodies and interacts directly with PML. J Cell Sci. 111(Pt 10),1319-29 (1998)
  20. ^ Borden, K.L., Freemont, P.S., The RING finger domain: a recent example of a sequence-structure family. Curr Opin Struct Biol. 6(3),395-401 (1996)
  21. ^ Freemont, P.S. RING for destruction? Curr Biol. 10(2), R84-87 (2000).
  22. ^ Crone, M.A. and Freemont, P.S. Simple Low-Cost Production of DNA MS2 Virus-Like Particles as Molecular Diagnostic Controls. GEN Biotechnol. 1(6), 496-503 (2022).
  23. ^ "SynbiCITE". synbicite.com. Retrieved 2023-02-15.



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