Stephen C. West

from Wikipedia, the free encyclopedia
Stephen C. West

Stephen Craig West (born April 11, 1952 in Hessle , Yorkshire ) is a British biochemist and molecular biologist.

West grew up near Hull in Yorkshire. His father was a fish seller and West says that he wanted to study primarily to avoid working with fish. He studied at the University of Newcastle with a bachelor's degree in 1974 and a doctorate in biochemistry in 1977. The subject of the dissertation was DNA repair ( DNA repair in Escherichia coli ), his later main research area. As a post-doctoral student he was with Paul Howard-Flanders at Yale University and from 1985 he had his own research group at the Imperial Cancer Research Fund (from 2002 Cancer Research UK) in Clare Hall in Hertfordshire, which merged with the Francis Crick Institute in 2016 . He is Senior Group Leader at the Francis Crick Institute in London and Honorary Professor at University College London and Imperial College London.

He was involved in unraveling the role of various enzymes in DNA repair in bacteria and eukaryotes. At Yale University he presented RecA in pure form and characterized the enzyme and its function in DNA recombination. He then examined the function of the enzymes of the RuvABC group (which dissolve Holliday structures in bacteria) in England and identified corresponding enzymes in eukaryotes such as GEN1 in humans. He was the first to present Rad51 purely for structural elucidation, the analogue of RecA in humans, and showed that it has a similar function to RecA. His laboratory succeeded in purifying and determining the structure of the BRCA2 protein and found that it is a chaperone for the binding of Rad51 to DNA. He also clarified the role of aprataxin as an enzyme that plays a role in DNA repair (it removes an adenosine monophosphate molecule from one end of the DNA in the event that an error occurred in the linkage of DNA strands, so try again Linkage can be started) and is defective in the case of a nerve disease (ataxia oculomotor apraxia).

In 2007 he received the Louis Jeantet Prize . He is a Fellow of the Royal Society (1995) and the Academy of Medical Sciences and an external member of the National Academy of Sciences (2016). In 1994 he became an EMBO member. Since 2000 he has been a member of the Academia Europaea .

Fonts

  • with T. Shahid, X. Zhang et al .: Structure and mechanism of action of the BRCA2 breast cancer tumor suppressor. Nature Struct Mol Biol., Volume 21, 2014, pp. 962-968.
  • with MG Blanco, J. Matos: Dual control of Yen1 nuclease activity and cellular localization by Cdk and Cdc14 prevents genome instability. Molecular Cell, Vol. 54, 2014, pp. 94-106.
  • with HD Wyatt, S. Sarbajna, J. Matos: Coordinated actions of SLX1-SLX4 and MUS81-EME1 for Holliday Junction resolution in human cells. Molecular Cell, Vol. 52, 2013, pp. 234-247
  • with J. Matos, MG Blanco, SL Maslen, JM Skehel: Regulatory control of the resolution of DNA recombination intermediates during meiosis and mitosis. Cell, Vol. 147, 2011, pp. 158-172
  • with T. Wechsler, S. Newman: Aberrant chromosome morphology in human cells defective for Holliday junction resolution. Nature, Volume 471, 2011, pp. 642-646

Web links

Individual evidence

  1. ^ Paul Gabrielsen, Profile of Stephen C. West , Proc. Nat. Acad., 2017