Christopher Berndsen, Ph.D.
Education, Honors, Awards
- Assistant Professor, James Madison University, Harrisonburg, VA (2012-present)
- Ruth L. Kirschstein National Research Service Award (2009 – 2011)
- Johns Hopkins University School of Medicine and the Howard Hughes Medical Institute (2008 – 2012)
- Ph.D., Biomolecular Chemistry, University of Wisconsin-Madison School of Medicine, Madison, WI (2008)
- American Heart Association Pre-Doctoral Fellow (2007 – 2008)
- B.S., Chemistry, Roanoke College, Roanoke, VA (2003)
Research InterestsThe effects of post-translational modification of protein lysine residues on cellular function focusing on:
- Mechanistic enzymology of the modifying proteins
- Chemical and Chemo-enzymatic methods to create substrates and/or inhibitors of modifying enzymes
- X-ray crystallography to determine the structure of modifying enzymes and their substrates
The presence of DNA damaging agents or moving from fed to fasting states requires the cell to respond to rapidly changing conditions. These changes require an efficient system to regulate the proteins that are involved in metabolism, damage repair, and the cell cycle. Rather than transcribe and translate a new protein in response to a new stimulus (which is VERY slow!), cells modify the amino acid side chains of existing proteins with chemical tags, resulting in a rapid change of protein function. These chemical tags include adding an entire protein known as the Ubiquitin and Ubiquitin-like proteins. Modifications by ubiquitin or a ubiquitin-like protein play important roles in almost every cellular pathway, with new roles for the modification found every year.
My research interest is the mechanism of the enzymes that add the ubiquitin like protein, Ufm1, onto other proteins. Using chemical, biochemical, biophysical and molecular biology techniques the lab will dissect and compare the functional mechanisms of Uf-mylation enzymes from humans and the human parasite, L. donovani. The goal is to identify differences in the mechanisms of the enzymes leading to treatments for leishmaniasis and other parasitic diseases.
Selected Recent Publications
- Berndsen CE, Wolberger C., "A spectrophotometric assay for conjugation of ubiquitin and ubiquitin-like proteins." (2011) Anal Biochem. Nov 1;418(1):102-10.
- Samara NL, Datta AB, Berndsen CE, Zhang X, Yao T, Cohen RE, Wolberger C. "Structural insights into the assembly and function of the SAGA deubiquitinating module." (2010) Science. May 21;328(5981):1025-9.
- Berndsen CE, Tsubota T, Lindner SE, Lee S, Holton JM, Kaufman PD, Keck JL, Denu JM. "Molecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75." (2008) Nat Struct Mol Biol. Sep;15(9):948-56.
- Tsubota T, Berndsen CE, Erkmann JA, Smith CL, Yang L, Freitas MA, Denu JM, Kaufman PD. "Histone H3-K56 acetylation is catalyzed by histone chaperone-dependent complexes. " (2007) Mol Cell. Mar 9;25(5):703-12.
- Berndsen CE, Selleck W, McBryant SJ, Hansen JC, Tan S, Denu JM. "Nucleosome recognition by the Piccolo NuA4 histone acetyltransferase complex." (2007) Biochemistry Feb 27;46(8):2091-9.
- Berndsen CE, Albaugh BN, Tan S, Denu JM. "Catalytic mechanism of a MYST family histone acetyltransferase. " (2007) Biochemistry Jan 23;46(3):623-9.