| Gisela Storz | |
| Nationality: | American |
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Gisela Storz is a microbiologist at the Eunice Kennedy Shriver National Institute of Child Health and Human Development (NICHD) at the National Institutes of Health (NIH). She is a member of the National Academy of Sciences.
Gisela "Gigi" Storz received a B.A. in biochemistry in 1984 from University of Colorado Boulder. She completed her Ph.D. in biochemistry from University of California, Berkeley in the laboratory of Bruce Ames in 1988, where she discovered that OxyR senses hydrogen peroxide stress in Escherichia coli oxidation response. She trained briefly as a postdoctoral fellow at the National Cancer Institute with Sankar Adhya in 1989 and at Harvard Medical School with Frederick M. Ausubel from 1989 to 1991.[1] She joined the National Institute of Child Health and Human Development at NIH in 1991 and is currently head of the Section on Environmental Gene Regulation.
Storz's research interests include the characterization of small non-coding RNA and small proteins of 50 amino acids or less.[2] [3] An early focus of her research was the study of redox-sensitive transcription factors and the bacterial and yeast responses to oxidative stress. She discovered that the activity of the Escherichia coli transcription factor OxyR, now a paradigm for other redox-sensitive proteins, is regulated by reversible disulfide bond formation and elucidated how disulfide bond formation controls the nuclear localization of the Saccharomyces cerevisiae transcription factor Yap1. As a result of her group's serendipitous detection of the OxyS RNA, one of the first small regulatory RNAs to be discovered, attention shifted to the genome-wide identification and characterization of small regulatory RNAs in the model organism Escherichia coli. Work on small RNAs in Dr. Storz's lab revealed that the RNA chaperone Hfq stimulates the pairing of the majority of the small RNAs with mRNA targets and that small RNAs are integral to most regulatory circuits in bacteria. While identifying these small RNAs, her lab discovered that some of these small RNAs encode small proteins that had previously been overlooked because they are not detected in many traditional biochemical assays and the corresponding genes are poorly annotated. Her research group demonstrated that one such small protein, AcrZ, binds to the multidrug efflux pump protein AcrB to affect its ability to export certain classes of antibiotics. The Storz lab currently seeks to identify and to characterize the function of other small proteins from Escherichia coli.