Education, Honors, Awards

  • Associate Professor, James Madison University, Harrisonburg, VA (2018-present)
  • Assistant Professor, James Madison University, Harrisonburg, VA (2012-2018)
  • 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 Interests

The 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

Research Description

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. The Berndsen lab studies the enzymes that catalyze modification of protein lysine side chains with ubiquitin, which is a protein, and lysine acetyltransferases (KATs).  Defects in acetylation and ubiquitination are linked to anemia, insomnia, and cancer therefore knowledge of the catalytic mechanism provides insight into the biochemical basis of these syndromes.  
 
We study the chemical mechanism of the ubiquitination and acetyltransfer enzymes through biochemical assays of protein function, X-ray crystallography and NMR of the protein structure, computer modeling, and other biochemical and biophysical techniques. 
 
A second project involves the protein Tetherin, which alters viral release from cells.  The activity of Tetherin has been linked to HIV, Ebola, Influenza, Herpes and other enveloped viruses.  We aim to study the structure of Tetherin and how viral proteins antagonize this structure leading to blocking of Tetherin's anti-viral budding activity.
 

Selected Recent Publications

  • Monroe JD, Pope LE, Breault JSBerndsen CE, Storm AR. Quaternary Structure, Salt Sensitivity, and Allosteric Regulation of β-AMYLASE2 From Arabidopsis thaliana Frontiers in Plant Science 2018; 9, 1176.
  • Hossain RA, Dunham NR, Enke RA, Berndsen CE In silico modeling of epigenetic-induced changes in photoreceptor cis-regulatory elements. Mol Vis. 2018 Mar 14;24:218-230.
  • Storm AR, Kohler MRBerndsen CE, Monroe JD. Glutathionylation Inhibits the Catalytic Activity of Arabidopsis β-Amylase3 but Not That of Paralog β-Amylase1. Biochemistry. 2018 Feb 6;57(5):711-721. doi: 10.1021/acs.biochem.7b01274.
  • Ozcan KABerndsen CE.  Bending of the BST-2 coiled-coil during viral budding. Proteins. 2017 Nov;85(11):2081-2087. doi: 10.1002/prot.25362
  • Padala P, Oweis W, Mashahreh B, Soudah N, Cohen-Kfir E, Todd EABerndsen CE, Wiener R. Novel insights into the interaction of UBA5 with UFM1 via a UFM1-interacting sequence. Sci Rep. 2017 Mar 30;7(1):508. doi:10.1038/s41598-017-00610-0.
  • Young BH, Caldwell TA, McKenzie AM, Kokhan O, Berndsen CE. Characterization of the structure and catalytic activity of Legionella pneumophila VipF. Proteins. 2016 Oct;84(10):1422-30. doi: 10.1002/prot.25087

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