User:Christopher Berndsen/Labinfo

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The Berndsen Laboratory at James Madison University

NMR Structure of the ubiquitin-like protein UFM1

Drag the structure with the mouse to rotate

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 such as 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

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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
  5. ↑ 26601948
  6. ↑ 26789136

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Christopher Berndsen

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