Peter Wright & Jane Dyson seminars in Birmingham UK - 11 October 2023

Those in the Birmingham area might be interested to join the following seminars next week hosted by Teresa Carlomagno:

Prof Peter Wright and Prof Jane Dyson

The Scripps Research Institute, La Jolla, California

will give two talks with titles

Role of Intrinsically Disordered Proteins in Allosteric Regulation of Transcription


Role of Protein Disorder and Dynamics in Signaling Pathways

When: Wednesday October 11th, 2023 at 1:00 pm and 1:45 pm

Where: University of Birmingham, Biosciences Building, Lecture Theatre NG08

Both Peter and Jane are prominent US scientists, both members of the National Academy of Science, who have made seminal contributions to understanding protein mechanisms and folding in various cellular functions. Below are the abstracts of their talks and their biographies.

Abstract: Role of Intrinsically Disordered Proteins in Allosteric Regulation of Transcription

Intrinsically disordered proteins (IDPs) are highly abundant in the human proteome and mediate critical regulatory functions in the cell. The lack of stable globular structure confers numerous functional advantages on IDPs, allowing them to exert an exquisite level of control over cellular signaling processes. Transcription factors are rich in intrinsically disordered regions (IDRs) that function synergistically with structured domains to regulate gene expression. The disordered N-terminal transactivation domain of p53 facilitates discrimination between cognate sites and the vastly more abundant non-cognate sites in the genome. Within the transactivation domain, Thr55 functions as a highly cooperative, phosphorylation-dependent switch that regulates both activation and termination of p53-mediated transcriptional programs during different stages of the cellular DNA damage response. To perform their cellular functions, IDPs must frequently compete for binding to shared interaction hubs. The negative feedback regulator CITED2 efficiently downregulates the hypoxic response by displacing, in a unidirectional, switch-like manner, the hypoxia inducible transcription factor HIF-1α from the TAZ1 domain of the transcriptional coactivators CBP and p300. Allosteric conformational changes in TAZ1 and the flexibility and multivalency of the HIF-1a and CITED2 activation domains are key determinants of unidirectionality of the switch.

Abstract: Role of Protein Disorder and Dynamics in Signaling Pathways

Intrinsically disordered proteins (IDPs) and disordered regions or domains of proteins (IDRs) occur throughout the eukaryotic proteome, as well as facilitating the function of many viruses. Protein disorder and flexibility is particularly important in signaling processes, where interactions must be highly specific but also reversible. Some of the most common transcription factors are partially or completely disordered, and where structured domains are present, the role of the disordered domains is vital to their function. Examples include p53, CREB and HIF-1α. Transcription factors with a greater degree of structure, such as NF-κB nevertheless employ dynamics and molecular flexibility to achieve their function. This lecture will focus on studies to evaluate the participation of disorder in the function of two systems, CREB and NF-κB.


Peter Wright is a Professor in the Department of Integrative Structural and Computational Biology and holds the Cecil H. and Ida M. Green Chair of Biomedical Research at The Scripps Research Institute. He received B.Sc., M.Sc. and Ph.D. degrees in Chemistry from the University of Auckland and undertook postdoctoral study at the University of Oxford, England. Dr. Wright joined the faculty of the Department of Inorganic Chemistry at the University of Sydney, Australia in 1976. He was appointed to the faculty of Scripps in 1984 as Professor, and held the post of Chairman of the Department of Molecular Biology from 1987-2012. He received an honorary M.D. degree from the Karolinska Institute, Sweden in 1995, and an honorary D.Sc. degree from the University of Sydney, Australia, in 2003. He is an elected fellow of the International Society of Magnetic Resonance, the NMR Society of Japan, the American Association for the Advancement of Science, and the American Academy of Arts and Sciences, and is a member of the National Academy of Sciences. He has received several awards including the Stein and Moore Award from the Protein Society and the ISMAR Prize from the International Society of Magnetic Resonance. His research interests are in applications of NMR to study mechanisms of protein folding and misfolding, the structural basis of protein-protein and protein-nucleic acid interactions in the regulation of gene expression, and the role of dynamics in protein function. His work on protein interactions led to the realization that many proteins are intrinsically disordered, and that protein disorder plays an important functional role in cellular signaling networks. He has acted as Editor-in-Chief of Journal of Molecular Biology since 1990.


Jane Dyson received the degree of B.Sc.(hons) from the University of Sydney in 1973 and a Ph.D. from the University of Sydney in 1977. She was a postdoctoral fellow at Massachusetts Institute of Technology from 1977-78, and held a Damon Runyon-Walter Winchell postdoctoral award. She was appointed as a Lecturer in Chemistry at the University of New South Wales in 1979, and joined the Scripps Research Institute in 1984, where she is presently a Professor. She is an elected fellow of the International Society of Magnetic Resonance. She received the degree of D.Sc. from the University of Sydney in 2009 and was awarded the 2019 ISMAR Prize from the International Society of Magnetic Resonance. She was elected to the National Academy of Sciences of the U.S.A. in 2022. She acted as the Editor-in-Chief of Biophysical Journal from 2017-2021. Her research interests are in the conformation of peptides, protein folding and dynamics, and structure and functional studies of proteins, both folded and intrinsically disordered, using NMR and other spectroscopic techniques.