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Ron Hay

Email: r.t.hay@dundee.ac.uk

Ron Hay was born and educated in Dundee and studied for a degree in Biochemistry at Heriot-Watt University, Edinburgh (1971-1975). He studied for his PhD at the Medical Research Council Virology Unit in Glasgow under the supervision of Dr John Hay working on replication of herpes simplex virus DNA (1975-1979).

A Damon Runyon-Walter Winchell Cancer Fund postdoctoral fellowship award allowed him to work in the laboratory of Dr Mel DePamphilis at Harvard Medical School, Boston where he determined the location and structure of RNA primers that initiate DNA replication at the Simian Virus 40 origin of replication (1979-1982).

Returning to the MRC Virology Unit he established his independent laboratory working on the initiation of adenovirus DNA replication (1982-1985). He then moved to the University of St. Andrews where he held Lecturer and Reader positions before taking up the Chair in Molecular Biology and became Deputy Director of the Centre for Biomolecular Sciences. In October 2005 he took up the Chair of Molecular Biology in the University of Dundee and is part of the Centre for Gene Regulation and Expression.

Ron’s research has established conjugation with the Small Ubiquitin-like Modifier (SUMO) as an important regulatory mechanism in eukaryotes. A key role for SUMO and ubiquitin was uncovered in mediating the effects of arsenic when it is used therapeutically in the treatment of Acute Promyelocytic Leukaemia. Recently determination of the structure of a RING E3 ligase and ubiquitin-loaded E2 complex primed for catalysis has revealed the mechanism of ubiquitin modification

Ron is a Wellcome Trust Senior Investigator and a fellow of the Royal Society, the Royal Society of Edinburgh, the Academy of Medical Sciences, Academia Europaea and is a member of the European Molecular Biology Organisation. In 2012 Ron was awarded the Novartis Medal and Prize of the Biochemical Society.

Selected Publications

Seifert A, Schofield P, Barton GJ, Hay RT. (2015) Proteotoxic stress reprograms the chromatin landscape of SUMO modification. Science Signaling. 8(384):rs7.

Branigan E, Plechanovová A, Jaffray EG, Naismith JH, Hay RT. (2015) Structural basis for the RING-catalyzed synthesis of K63-linked ubiquitin chains. Nature Structural and Molecular Biology. (8):597-602.

Pelisch F, Sonneville R, Pourkarimi E, Agostinho A, Blow JJ, Gartner A, Hay RT. (2014) Dynamic SUMO modification regulates mitotic chromosome assembly and cell cycle progression in Caenorhabditis elegans. Nature Communications. 5:5485.

Tammsalu T, Matic I, Jaffray EG, Ibrahim AF, Tatham MH, Hay RT. (2014) Proteome-wide identification of SUMO2 modification sites. Science Signaling.7(323):rs2.

Plechanovovà A, Jaffray E, Tatham MH, Naismith JH, Hay RT. (2012) Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis. Nature 489, 115-120

Yin Y, Seifert A, Chua JS, Maure J-F, Golebiowski F, Hay RT. (2012) SUMO-targeted ubiquitin E3 ligase RNF4 is required for the response of human cells to DNA damage Genes and Development 26:1196-1208

Plechanovova A, Jaffray EG, McMahon SA, Johnson KA, Navratilova I, Naismith JH, Hay RT. (2011) Mechanism of ubiquitylation by dimeric RING ligase RNF4. Nature Structural and Molecular Biology 18:1052-9

Tatham MH, Matic I, Mann M, Hay RT. (2011) Comparative Proteomic Analysis Identifies a Role for SUMO in Protein Quality Control. Science Signaling 4: rs4.

Golebiowski F, Matic I, Tatham MH, Cole C, Yin Y, Nakamura A, Cox J, Barton GJ, Mann M, Hay RT. System-wide changes to SUMO modifications in response to heat shock. (2009) Science Signaling. 2: ra24.

Tatham MH, Geoffroy MC, Shen L, Plechanovova A, Hattersley N, Jaffray EG, Palvimo JJ, Hay RT. (2008) RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation. Nature Cell Biology. 10: 538-546.

A full list of publications can be found here.

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