Cynthia Wolberger

Dr. Cynthia Wolberger's pioneering structural and biochemical studies have laid the groundwork for understanding the mechanisms of eukaryotic transcriptional regulation and ubiquitin signaling. Her work on combinatorial regulation of transcription established the molecular principles by which multiprotein complexes coordinate DNA recognition and gene regulation in response to multiple cellular signals. In studies of the NAD⁺-dependent sirtuin family of histone deacetylases, she used innovative approaches to trap the enzyme in multiple states and thereby elucidate the structure-based mechanism of this novel reaction. In her work on ubiquitin signaling, Dr. Wolberger broke new ground by elucidating how a polyubiquitin chain with a particular linkage type can be assembled, how different linkages influence the conformations these chains can adopt, and how the enzymes that disassemble specific chains are regulated. In work that combines her interests in both transcription and ubiquitination, she has elucidated mechanisms by which histone ubiquitination plays a signaling role in regulating transcription. Her ground-breaking structural studies of enzyme complexes bound to ubiquitinated nucleosomes have revealed the molecular basis for recognition of specific histone ubiquitination sites and the mechanism of cross-talk between histone ubiquitination and methylation. This work has uncovered unexpected plasticity in the nucleosome core that has exciting implications for understanding histone modifications and nucleosome dynamics. In addition to her outstanding research, she has served in leadership roles at the institutional and national levels. At Johns Hopkins University, she spearheaded a major study of gender equity that has had a far-reaching and highly beneficial impact. Nationally, she has been a leader in the structural biology community, an influential educator, and an advocate for openness in scientific communication.