Sanchita Hati

Associate Professor

Office: Phillips-445
Phone: 715 836 3850
Email: hatis at uwec dot edu

               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

Teaching Interests

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 investigating the domain motions and exploring if the communication among the various domains of an ARS can be accomplished through cooperativities of these domain motions.


Grants and Fellowships

NIH Recovery Act Administrative Supplement Award, 2010

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

Recent Publications

31. Probing the Global and Local Dynamics of Aminoacyl-tRNA Synthetases using All-atom and Coarse-grained Simulations.  A. M. Strom, S. C. Fehling, S. Bhattacharyya, and S. Hati (2014), J. Molecular  Modeling, 2235.

30.  Comparison of the Intrinsic Dynamics of Aminoacyl-tRNA Synthetases. N. Warren, A. Strom, B. Nicolet, K. Albin, J. Albrecht, B. Bausch, M. Dobbe, M. Dudek, S. Firgens, C. Fritsche, A. Gunderson, J. Heimann, C. Her, J. Hurt, D. Konorev, M. Lively, S. Meacham, V.Rodriguez, S.Tadayon, D. Trcka, Y. Yang, S. Bhattacharyya, and S. Hati (2014) The Protein Journal, 184-198.

29. Strictly conserved lysine of prolyl-tRNA synthetase editing domain facilitates binding and positioning of misacylated tRNAPro. T. G. Bartholow, B. L. Sanford, B. Cao, H. L. Schmit, J. M. Johnson, J. Meitzner, S. Bhattacharyya, K. Musier-Forsyth, and S. Hati (2014) Biochemistry, 53,1059-1068.

28. Multiple pathways promote dynamical coupling between catalytic domains in Escherichia coli prolyl-tRNA synthetase. J. M. Johnson, B. L. Sanford, A. M. Strom, S. N. Tadayon, B. P. Lehman, A. M. Zirbes, S. Bhattacharyya, K. Musier-Forsyth, and S. Hati (2013) Biochemistry, 52, 4399-4412.

27. Role of coupled motions in the catalytic activity of prokaryotic-like prolyl-tRNA synthetases. B. L. Sanford, B. V. Cao, J. M. Johnson, K. Zimmerman, A. M. Storm, R. M. Mueller, S. Bhattacharyya, K. Musier-Forsyth, and S. Hati (2012) Biochemistry, 51, 2146-2156.

26. Interplay of flavin's redox states and protein dynamics: an insight from QM/MM simulations of dihydronicotinamide riboside quinone oxidoreductase 2. R. M. Mueller, M. A. North, C. Yang, S. Hati, and S. Bhattacharyya (2011) J. Phys. Chem. B, 115, 3632-3641.

25. 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., 284, 10088-10099.

24. 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.

23. 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.