Sanchita Hati Assistant Professor Office: Phillips-445 Phone: 715 836 3850 Email: hatis at uwec dot edu

       Education

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Teaching Interests
 

• Biophysical Chemistry

• Biochemistry

• General Chemistry

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Research Interests

Cooperative domain motions in enzymes
 

Exploring the role of  domain motions on the enzymatic function of aminoacyl-tRNA synthetases (ARSs)  It has been observed that various domains in ARSs, though situated distantly, coordinate with each other for carrying out the enzymatic function with great precision.  However, the molecular mechanism of this interdomain coordination in ARSs has remained poorly understood. How do these domains communicate with each other? Does  protein dynamics play a role on these long-range communications? Do these communications propagate through space? To explore these questions we are currently studying the domain motions in two ARSs, the class I leucyl-tRNA synthetase and class II prolyl-tRNA synthetase. We are studying the domain motions and exploring if the communication among the various domains of an ARS can be accomplished through cooperativities of these domain motions.

 
 

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Awards and Honors

         NIH Academic Research Enhancement Award, 2008

         Research Corporation Cottrell College Science Award, 2006

         Graduate Research Fellowship, Indian Association for the Cultivation of Science, India, 1991

         Lectureship and Research Fellowship Award in Chemistry, University Grant Commission, India,1991

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Selected Publications
 

1. Evolutionary basis for the coupled-domain motions in Thermus thermophilus leucyl-tRNA synthetase. K. M. Weimer, B. L. Shane, M. Brunetto, S. Bhattacharyya, and S. Hati. (2009) J. Biol. Chem., in press.

2. Restoring species-specific posttransfer editing activity to a synthetase with a defunct editing domain.  J. SternJohn, S. Hati, P. G. Siliciano, and K. Musier-Forsyth (2007) Proc. Natl. Acad. Sci. USA, 104, 2127-32.

3. Pre-transfer editing by class II prolyl-tRNA synthetase: role of aminoacylation active site in “selective release” of noncognate amino acids. S. Hati, B. Ziervogel, J. SternJohn, F. C. Wong, M. C. Nagan, A. R. Rosen, P. G. Siliciano, J. Chihade, and K. Musier-Forsyth. (2006) J. Biol. Chem. 281, 27862-27872.

4. Nickel²⁺- mediated assembly of an RNA-amino acid complex. S. Hati, A. R. Boles, J. M. Zaborske, B. Bergman, A. L. Posto, and D. H. Burke. (2003) Chem. and Biol.  10, 1129-1137.

5. Comparative modeling of the phosphatase and kinase domains of protein tyrosine phosphatase and insulin receptor kinase from Drosophila melanogaster (DPTP61fm) and a computational study of their mutual interactions. S. Hati, S. Bhattacharyya, J. V. Price, and A. S. Tracey. (2002) Biochemistry and Cell Biology 80, 225-239.