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Research Interests: Mechanism of ubiquitin signaling in transcription and the DNA damage response; Structural and biochemical studies of enzyme complexes involved in ubiquitin signaling and chromatin modification; cross-talk between histone modifications. ...read more
Dr. Cynthia Wolberger is a professor of biophysics and biophysical chemistry at the Johns Hopkins University School of Medicine. Her research focuses on structural biology, ubiquitin signaling and regulation of transcription.
Dr. Wolberger received her undergraduate degree from Cornell University and earned her Ph.D. at Harvard University. She completed postdoctoral work at the University of California, San Francisco, and the Johns Hopkins School of Medicine. Dr. Wolberger joined the Johns Hopkins faculty in 1991.
Dr. Wolberger studies how DNA packaging proteins—which coil DNA into neat, compact bundles in the cell—turn genes on or off, or initiate broken DNA repair. These DNA packaging proteins, aka histones, are called to action by the addition of chemical tags, like ubiquitin protein or acetyl chemical groups. To determine the structure of the histones and which chemical tags they use, Dr. Wolberger employs x-ray crystallography, a technique that allows researchers to develop three-dimensional models of proteins.
Dr. Wolberger is a Fellow of the American Association for the Advancement of Science. She has been recognized with the Dorothy Crowfoot Hodgkin Award by The Protein Society for her work in determining the structure of proteins involved in transcriptional regulation.
Dr. Wolberger and her lab are interested in the structural and mechanistic basis for transcriptional regulation and ubiquitin signaling. Protein function is dynamically regulated in the cell by the attachment and subsequent removal of covalent posttranslational modifications. Acetylation and ubiquitination both occur in chromatin, the nucleoprotein complex into which eukaryotic DNA is packaged. Acetylation of the histone proteins in chromatin is associated with activation of transcription, whereas ubiquitination can be either an activating or a repressive mark, depending on which histone protein is modified. Ubiquitination of chromatin also plays a role in the response to DNA double-strand breaks, helping to recruit proteins that are required for DNA repair. They are interested in the molecular basis for these events, which ensure the integrity and expression of the genome. They use x-ray crystallography, enzymology, and a variety of biophysical tools to gain insights into the mechanisms underlying these essential cellular processes.
Lab Website: Wolberger Lab
Morgan M, Haj-Yahya M, Ringel AE, Bandi P, Brik A, Wolberger C. (2016) Structural basis for histone H2B deubiquitination by the SAGA DUB module. Science 351:725-8.
Wiener R, Zhang X, Wang T, Wolberger C. (2012) The mechanism of OTUB1-mediated inhibition of ubiquitination. Nature. 483:618-22.
Samara NL, Datta AB, Berndsen CE, Zhang X, Yao T, Cohen RE, Wolberger C (2010) Structural insights into the assembly and function of the SAGA deubiquitinating module. Science 328: 1025-1029.
A.P. VanDemark, R.M. Hofmann, C. Tsui, C.M. Pickart and C. Wolberger (2001) Molecular Insights into Polyubiquitin Chain Assembly. Crystal Structure of the Mms2/Ubc13 Heterodimer. Cell 105:711-720.
Ringel AE, Cieniewicz AM, Taverna SD, Wolberger C. (2015) Nucleosome competition reveals processive acetylation by the SAGA HAT module. Proc Natl Acad Sci U S A. 112(40):E5461-70.
Program in Biochemistry, Cellular and Molecular Biology (BCMB)
Program in Molecular Biophysics (PMB)
Chemistry-Biology Interface (CBI)
Discoveries - ubiquitin signaling
Cynthia Wolberger on ubiquitin and Candid Camera (Fundamentals)
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