User:Christopher Berndsen/Labinfo
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Laboratory Overview
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The Berndsen Lab is located in the Department of Chemistry and Biochemistry at James Madison University in Harrisonburg, VA. The primary research focus is the mechanism enzymes involved in the conjugation and processing of ubiquitin and ubiquitin-like proteins. Additionally, the lab is interested in integrating protein structure research and molecular basis for disease into the biochemistry classroom.
Research Highlights
Ubiquitin and Ubiquitin-like proteins are linked to many cellular functions included protein degradation and DNA damage repair [1][2]. The Berndsen Lab is interested in the catalytic mechanisms the conjugating enzymes E1, E2, and E3 use to attach ubiquitin/ubiquitin-like proteins to the substrate lysine. We are also interested in the proteases that remove these modifications and the chemical mechanism(s) of catalysis. We are currently focused on UFM1 conjugation and the E1 enzyme associated with UFM1, UBA5.
We have also worked on proteins associated with ubiquitin including Ubc13 [3][4], AMSH [5], and YUH1.
In addition to our work on enzyme mechanism, we have worked on the structure mechanism of viral tethering by the human protein, BST-2. Recently, we proposed how the disulfides of BST-2 function to increase the strength of BST-2 during viral tethering [6].
Educational Activities
The Berndsen lab has also taken an active role in using Proteopedia in the Biochemistry classroom and have students use protein structure prediction to understand the molecular basis for disease.
2015 Proteopedia Projects
How Gluten Stimulates an Immune Response
Previous Projects
References
- ↑ Pickart CM, Eddins MJ. Ubiquitin: structures, functions, mechanisms. Biochim Biophys Acta. 2004 Nov 29;1695(1-3):55-72. PMID:15571809 doi:http://dx.doi.org/10.1016/j.bbamcr.2004.09.019
- ↑ Berndsen CE, Wolberger C. New insights into ubiquitin E3 ligase mechanism. Nat Struct Mol Biol. 2014 Apr;21(4):301-7. doi: 10.1038/nsmb.2780. PMID:24699078 doi:http://dx.doi.org/10.1038/nsmb.2780
- ↑ Putney DR, Todd EA, Berndsen CE, Wright NT. Chemical shift assignments for S. cerevisiae Ubc13. Biomol NMR Assign. 2015 Oct;9(2):407-10. doi: 10.1007/s12104-015-9619-x. Epub, 2015 May 7. PMID:25947351 doi:http://dx.doi.org/10.1007/s12104-015-9619-x
- ↑ Berndsen CE, Wiener R, Yu IW, Ringel AE, Wolberger C. A conserved asparagine has a structural role in ubiquitin-conjugating enzymes. Nat Chem Biol. 2013 Mar;9(3):154-6. doi: 10.1038/nchembio.1159. Epub 2013 Jan 6. PMID:23292652 doi:10.1038/nchembio.1159
- ↑ Baiady N, Padala P, Mashahreh B, Cohen-Kfir E, Todd EA, Du Pont KE, Berndsen CE, Wiener R. The Vps27/Hrs/STAM (VHS) Domain of the Signal-transducing Adaptor Molecule (STAM) Directs Associated Molecule with the SH3 Domain of STAM (AMSH) Specificity to Longer Ubiquitin Chains and Dictates the Position of Cleavage. J Biol Chem. 2016 Jan 22;291(4):2033-42. doi: 10.1074/jbc.M115.689869. Epub 2015 , Nov 24. PMID:26601948 doi:http://dx.doi.org/10.1074/jbc.M115.689869
- ↑ Du Pont KE, McKenzie AM, Kokhan O, Sumner I, Berndsen CE. The Disulfide Bonds within BST-2 Enhance Tensile Strength during Viral Tethering. Biochemistry. 2016 Feb 16;55(6):940-7. doi: 10.1021/acs.biochem.5b01362. Epub, 2016 Feb 4. PMID:26789136 doi:http://dx.doi.org/10.1021/acs.biochem.5b01362
