Thomas was born in Treboeth, Swansea to John Robert and Lorna (née Harris) Thomas, and she attended Llwyn-y-Bryn High School for Girls. She continued her education at University College of Swansea where she received a first class Bachelor of Science degree in chemistry in 1964 followed by a PhD in 1967. Her thesis was on Hydroxyl-carbonyl interaction in cyclic peptides and depsipeptides.[3]
Career and research
After her PhD in 1967, Thomas remained with Cambridge at Darwin College until 1969. During this time, she held a Beit Memorial Fellowship for Medical Research at the Medical Research Council (MRC) Laboratory of Molecular Biology (LMB), a lab dedicated to understanding biological processes in order to solve major problems in human disease.[6] She then served as a member of the university academic staff as well as a Fellow of New Hall, now Murray Edwards College, where she acted as vice president from 1983 to 1987. In 1985, during her time as vice president of New Hall, she received her degree of Doctor of Science from the University of Cambridge.[7]
Thomas is a professor emerita of macromolecular biochemistry at Cambridge and has been a professor there since 1991. She acted as chairman of the Cambridge Centre for Molecular Recognition between 1993 and 2003.[7] In 2007, Thomas became a fellow of St. Catharine's College, and in 2016, she became an honorary fellow. She was elected as the 38th master of St. Catharine's College in 2007, making her the first female master since the college was founded in 1473. Elected by the president and fellows of the college, she remained master until 2016, when she was succeeded by Professor Sir Mark Welland.[8] A scholarship fund called the Jean Thomas PhD Award was created in her honour by alumnus of St. Catharine's Peter Dawson. It grants one fully funded PhD studentship per year to a student at St. Catharine's.[9]
Thomas's recent work has focused on the in-depth understanding of chromatin proteins, such as high-mobility group box 1 protein (HMGB1) and histone H1, and their interactions with DNA. In 2007, her research team used NMR mapping to better define the negative regulation of the HMGB1-DNA interaction that was suspected to be largely controlled by the acidic tail of HMGB1. They found that regardless of the length of the acidic tail, it makes extensive contacts with the DNA-binding regions of the two tandem HMG-boxes in HMGB1.[15] A year later, she published a paper describing the opposing effects of H1 and HMGB1 on the nucleosome. Histone H1 was shown to stabilize the structure by winding two turns of linker DNA around the octamer while HMGB1 destabilized the nucleosome by bending adjacent DNA. NMR spectroscopy was again used to show that H1 binds to the acidic tail of HMGB1 via its basic C-terminus, thus halting the HMGB1-DNA interaction.[16] She later described the structure of these interactions as collapsed and sandwich-like, suggesting that it is important for the dynamic activity of the DNA-binding proteins.[17]
Thomas also found that HMGB1 plays a role as a chaperone in the binding of transcription factors like p53 to DNA. In 2012, again using NMR spectroscopy, her team solved the structure of the A-box/p53 complex formed by the interaction between the N-terminus of p53 and a single HMG-box of HMGB1.[18] Recently, she studied proteins from Drosophila melanogaster and maize that are analogous to HMGB1 in order to describe a simpler, general mechanism of the self-inhibitive behavior of the DNA-binding regions of the HMG-boxes in HMGB1.[19] She currently continues to lead a team of researchers in the Department of Biochemistry at the University of Cambridge.[20]
^Watson, M; Stott, K; Thomas, JO (14 December 2007). "Mapping intramolecular interactions between domains in HMGB1 using a tail-truncation approach". Journal of Molecular Biology. 374 (5): 1286–97. doi:10.1016/j.jmb.2007.09.075. PMID17988686.
^Cato, L; Watson, M; Stott, K; Thomas, JO (31 December 2008). "The interaction of HMGB1 and linker histones occurs through their acidic and basic tails". Journal of Molecular Biology. 384 (5): 1262–72. doi:10.1016/j.jmb.2008.10.001. PMID18948112.
^Stott, K; Watson, M; Howe, F; Grossman, JG; Thomas, JO (12 November 2010). "Tail-mediated collapse of HMGB1 is dynamic and occurs via differential binding of the acidic tail to the A and B domains". Journal of Molecular Biology. 403 (5): 706–22. doi:10.1016/j.jmb.2010.07.045. PMID20691192.