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Anthony Blaszczyk, Recipient of The Robert T. Simpson Award

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May 22, 2017 –Anthony Blaszczyk, graduate student in biochemistry, microbiology and molecular biology has been awarded the 2017 Robert T. Simpson Graduate Student Award for Innovative (Risky) Science.  The award will be presented at the Robert T. Simpson Memorial Lecture in Molecular Medicine at 4:00 pm on May 25, 2017 in 100 Huck Life Sciences Building on the Penn State, University Park, campus.

The Graduate Student Award for Innovative (Risky) Science was created by the family of Robert T. Simpson in 2005 in memory of the former professor of biochemistry and molecular biology.  Simpson embraced the concept of high-risk, high-impact research.  The award was therefore established to recognize an individual graduate student, working under the direction of a biochemistry and molecular biology faculty member, who has made important and innovative contributions in forwarding their research in their specific area of study.


Blaszczyk conducts his research in the laboratory of Squire Booker, professor of chemistry and of biochemistry and molecular biology.  The Booker Laboratory is interested in elucidating the mechanisms by which enzymes catalyze the methylation of unactivated C-H bonds, which is a burgeoning area of biochemical research. Blaszczyk focuses his research on one subset of enzymes, known as Class B radical SAM methylases, which, in addition to a [4Fe-4S] cluster, require an additional cobalamin cofactor for catalysis. Although these enzymes play crucial roles in the biosynthetic pathway of many antibiotics, mechanistic studies have been hampered due to their inherent insolubility upon overproduction in the bacteria, Escherichia coli.


In his studies, Blaszczyk has developed a procedure for the overproduction and purification of a Class B radical SAM methylase TsrM that, for the very first time, produces soluble protein that can be purified to near homogeneity with both its cobalamin and iron-sulfur cofactors intact. TsrM catalyzes the methylation of the C2 position of the indole ring of tryptophan, which is the first step in the biosynthesis of the thiopeptide antibiotic, Thiostrepton A.


Blaszczyk’s studies on TsrM have revealed it to be an outlier in the radical SAM superfamily, because, unlike all other radical SAM enzymes, it does not reductively cleave SAM to generate a 5’-dA•. Spectroscopic studies on TsrM reveal the cobalamin cofactor to bind in an uncharacteristic five-coordinate base-off conformation that, only upon addition of SAM, is converted to a pseudo-four coordinate cobalamin species. His work has provided strong evidence to suggest that TsrM catalyzes its reaction via a polar mechanism involving two SN2 displacements, which is a vastly different mechanism than was previously proposed.


Simpson was an international leader for more than 35 years in research on chromatin, a fundamental component of chromosomes, and its role in gene regulation.  Simpson was at the NIH from 1970 until 1995, when he became the Verne M. Willaman Professor of Molecular Biology at Penn State. His addition to Penn State in 1995 is considered to have placed Penn State and the Department of Biochemistry and Molecular Biology at the forefront of chromatin research and to have greatly enhanced Penn State's research and educational missions.