Cynthia Wolberger

Johns Hopkins University


Primary Section: 29, Biophysics and Computational Biology
Secondary Section: 21, Biochemistry
Membership Type: Member (elected 2019)

Biosketch

Cynthia Wolberger is a structural biologist recognized for her work on the mechanisms underlying transcriptional regulation and ubiquitin signaling. She is known particularly for her work on the mechanisms underlying combinatorial regulation of transcription and the role of histone ubiquitination in modulating transcription and chromatin dynamics. She has also elucidated the molecular basis for assembly and cleavage of polyubiquitin chains of particular linkage types. Wolberger was born and raised in New York City, where she attended the Bronx High School of Science. After receiving her undergraduate degree in physics from Cornell University and a Ph.D. in biophysics from Harvard University, she was a postdoctoral fellow at the University of California, San Francisco and at the Johns Hopkins University School of Medicine. She joined the faculty of the Johns Hopkins School of Medicine Department of Biophysics and Biophysical Chemistry in 1991. She was named a David and Lucile Packard Fellow in Science and Engineering. Wolberger is a recipient of the Protein Society's Dorothy Crowfoot Hodgkin award and is a fellow of the American Association for the Advancement of Science. She is a member of both the American Academy of Arts and Sciences and the National Academy of Sciences.

Research Interests

Cynthia Wolberger's laboratory is focused on the molecular mechanisms by which genes are regulated and how attachment of the small protein, ubiquitin, regulates transcription and the response to DNA damage. Her research combines macromolecular structure determination, enzymology, biochemistry and biophysical methods to study the macromolecular complexes that orchestrate these processes. Her studies of multiprotein complexes bound to DNA revealed the molecular basis of combinatorial regulation of gene expression. In work on the sirtuin family of histone deacetylase enzymes, her group elucidated the structure-based mechanism of these enzymes' unusual NAD+ -dependent deacetylation mechanism by capturing structural snapshots of the enzymes at different points in the reaction. Her group elucidated how polyubiquitin chains with a particular linkage type are assembled and how the deubiquitinating enzymes that disassemble these chains are regulated. A current focus is on mechanisms by which histone ubiquitination regulates transcription and chromatin dynamics, and how cross-talk between ubiquitination and other histone modifications establishes different chromatin states.

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