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Jane Dyson, PhD

Professor Emeritus

Department of Integrative Structural and Computational Biology

Jane Dyson, PhD

Research Focus

NMR is the method of choice in studying unfolded proteins, as well as proteins such as the prion protein that have highly disordered parts. Since many of the entries in the published genomes appear to code for proteins that should be intrinsically unstructured, an understanding of the nature and behavior of unfolded proteins is assuming increasing importance. Many important proteins contain disordered or dynamic regions, making structure determination by X-ray crystallography and cryo-EM difficult. Incorporation of NMR studies into the determination of the structure and function of molecular machines can define not only structures of flexible portions but can give insights into the role of molecular motions and disorder into the function of the machine. We have used such a combined approach to examine the complexes of the transcriptiion factor NF-kappaB with DNA and with its inhibitor IkappaB. These studies have led to new insights into the mechanisms by which NF-kappaB transcriptional activation is turned on and off. Another major emphasis in the lab is on the interactions of chaperones with their client proteins and co-chaperones. Again a combined approach using NMR gives new information on these dynamic and heterogeneous systems.

Links

Structure of Important Tumor Growth Protein--A Target for Cancer Therapy-- Solved at The Scripps Research Institute (TSRI)

Select Publications

  • Wright, Peter E.; Dyson, H. J. Intrinsically disordered proteins in cellular signalling and regulation. Nature Reviews Molecular Cell Biology 2015, 16, 18-29.

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  • Mukherjee, S. P.; Quintas, P. O.; McNulty, R.; Komives, E. A.; Dyson, H. J. Structural characterization of the ternary complex that mediates termination of NF-?B signaling by I?Ba. Proceedings of the National Academy of Sciences of the United States of America 2016, 113, 6212-6217.

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  • Dyson, H J.; Wright, Peter E. How Does Your Protein Fold? Elucidating the Apomyoglobin Folding Pathway.. Accounts of chemical research 2017, 105-111.

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  • Wu, H.; Hyun, J.; Martinez-Yamout, M. A.; Park, S. J.; Dyson, H. J. Characterization of an Hsp90-Independent Interaction between Co-Chaperone p23 and Transcription Factor p53. Biochemistry 2018, 57, 935-944.

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  • Risør, Michael W.; Jansma, Ariane L.; Medici, Natasha; Thomas, Brittany; Dyson, H J.; Wright, P E. Characterization of the High-Affinity Fuzzy Complex between the Disordered Domain of the E7 Oncoprotein from High-Risk HPV and the TAZ2 Domain of CBP. 2021, 60, 3887-3898.

  • Singh, Amrinder; Martinez-Yamout, M A.; Wright, P E.; Dyson, H J. Structural and dynamic studies of DNA recognition by NF-?B p50 RHR homodimer using methyl NMR spectroscopy. 2022, 50, 7147-7160.
News, Events & Media
Three Scripps Research faculty elected to National Academy of Sciences
News

Three Scripps Research faculty elected to National Academy of Sciences

Hollis Cline, Jane Dyson and James Williamson among newly announced members.

Institute News
In the Battle for Real Estate, a Disordered Protein Wins Out
News

In the Battle for Real Estate, a Disordered Protein Wins Out

"This work at the molecular level has a real potential to benefit patients."

Integrative Structural & Computational Biology
Groundbreaking Science.
Life-changing Medicine.