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Assistant Professor
Office: Phillips-445
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Teaching Interests
General Chemistry Biochemistry Research Interests Cooperative domain motions in enzymes
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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 HonorsResearch 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 Publications1. 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.