Karin Musier-Forsyth
Professor and Ohio Eminent Scholar, Dept. of Chemistry & Biochemistry
3033 McPherson Lab
100 West 18th
Columbus, Ohio
43210
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Areas of Expertise
- Biochemistry
Education
- Ph.D., 1989, Cornell University, Biophysical Chemistry
- Postdoctoral, MIT, 1989-1992
Current Projects:
1. Role of host factor tRNAs and aminoacyl-tRNA synthetases in retroviral lifecyles: mechanism and inhibitor development.
2. Nucleic acid chaperone activity of retroviral Gag and Nucleocapsid proteins.
3. Quality control in protein synthesis: Editing function of prolyl-tRNA synthetases and free-standing synthetase-like domains.
Recent publications:
- Matrix domain modulates HIV-1 Gag’s nucleic acid chaperone activity via inositol phosphate binding. Christopher Jones, Siddhartha A. Datta, Alan Rein, Ioulia Rouzina, and Karin Musier-Forsyth (2011) J. Virol. 85: 1594-1603
- Features of double-stranded RNA-binding domains of RNA helicase A are necessary for selective recognition and translation of complex mRNAs. Arnaz Ranji, Nikolozi Shkriabai, Mamuka Kvaratskhelia, Karin Musier-Forsyth, and Kathleen Boris-Lawrie (2011) J. Biol. Chem. 286: 5328-5337.
- FRET analysis reveals distinct conformations of IN tetramers in the presence of viral DNA or LEDGF/p7. Jacques J. Kessl, Min Li, Michael Ignatov, Nikolozi Shkriabai, Jocelyn Eidahl, Lei Feng, Karin Musier-Forsyth, Robert Craigie, Mamuka Kvaratskhelia (2011) Nucleic Acids Res., 39: 9009-9022.
- Substrate-mediated fidelity mechanism ensures accurate decoding of proline codons. Byung Ran So, Songon An, Sandeep Kumar, Mom Das, Daniel A. Turner, Christopher M. Hadad, and Karin Musier-Forsyth (2011) J. Biol. Chem. 286: 31810-31820
- Substrate specificity of bacterial prolyl-tRNA synthetase editing domain is controlled by a tunable hydrophobic pocket. Sandeep Kumar, Mom Das, Christopher M. Hadad, and Karin Musier-Forsyth (2012) J. Biol. Chem., in press.