Sanchita Hati

Assistant Professor
 
 
 
 
 
 
 
 
 
 

Office: Phillips-445
Phone: 715 836 3850
Email: hatis at uwec dot edu
        Education
                BS, Burdwan University, Burdwan, India,1989
                MS, Burdwan University, Burdwan, India,1991
                Ph.D., Indian Association for the Cultivation of Science, Jadavpur University, Jadavpur, India,1997
 
 
Courses
Research
People
Publications
Resources

Teaching Interests
 
  • General Chemistry
  • Biochemistry
    • 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.

     
     


    Awards and Honors

             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


    Selected Publications

    1. 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.

    2. 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.

    3. 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.

    (Prof. M. Yarus, Department of Molecular, Cellular and Developmental Biology, University of Colorado wrote a preface of this work: “RNA as multitude/RNA as one”, Chem. Biol., 2003, 10, 1146-1148).

    4. 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.

    5. Interactions of vanadate with a-hydroxycarboxylic acids. S. Hati, R. J. Batchelor, F. W. B. Einstein and A. S. Tracey. (2001) Inorg. Chem. 40, 6258-6265.