Postdoctoral Position in Structural Enzymology, University of Michigan, Ann Arbor, MI, USA

A postdoctoral research position is available at the University of Michigan to study enzymes that regulate chromatin structure and function. The enzymes under investigation govern gene expression and other genomic functions by catalyzing post-translational modifications of target proteins such as histones and transcription factors. Specific examples of enzymes that are being studied include histone methyltransferases and histone demethylases. Aberrant expression, genetic rearrangements, or deletions of genes encoding histone-modifying enzymes frequently occur in cancer; thus, many of these proteins are targets for therapeutic intervention. Utilizing a combination of X-ray crystallography and biochemistry, we are characterizing the structure and function of these enzymes to gain insight into the mechanisms by which they regulate gene expression and how their dysregulation contributes to human diseases.

Research Facilities: Our laboratory is equipped with standard instrumentation for protein purification, characterization, and crystallization, including two AKTA chromatography systems, a VP-ITC isothermal titration calorimeter, and a Tecan microplate reader. In addition, we have access to the University’s Center for Structural Biology that hosts X-ray diffraction equipment and automated facilities for high-throughput cloning, protein expression screening, and protein crystallization (http://lsi.umich.edu/facultyresearch/centers/structuralbiology). Finally, the University of Michigan is a partner in the LS-CAT beamline at the Advanced Photon Source Synchrotron (located 4 hours away), providing us with access to a state-of-the-art beamline for macromolecular crystallography (www.ls-cat.org).

Qualifications: Applicants should have completed a Ph.D. in biochemistry, biophysics, chemistry, or a related field with 0-2 years postdoctoral research experience; prior training in X-ray crystallography and/or enzymology is desirable. Funding for this position is available through 2011, although applicants will be encouraged to apply for external support.

Recent Publications:
1. Couture JF, Collazo E, Ortiz-Tello PA, Brunzelle JS, & Trievel RC. (2007) Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase. Nat Struct Mol Biol. 14: 689-95. 2. Couture J.F., Collazo E., & Trievel R.C. (2006) Molecular recognition of histone H3 by the WD40 protein WDR5. Nat Struct Mol Biol. 13: 698-703. 3. Couture J.F., Collazo E., Hauk G., & Trievel R.C. (2006) Structural basis for the methylation site specificity of SET7/9. Nat Struct Mol Biol. 13: 140-146. 4. Couture J.F., Collazo E., Brunzelle J.S., & Trievel R.C. (2005) Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase. Genes Dev. 19: 1455-1465.


Please Submit: Cover letter, CV, brief description of previous research experience, and 3 reference letters to:

Dr. Raymond Trievel
Department of Biological Chemistry
University of Michigan
1150 West Medical Center Drive
5301 Medical Science Research Building III
Ann Arbor, MI 48109-0606
Email address: [EMAIL PROTECTED]
Fax number: 734-763-4581

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