- Biophysical Chemistry
- General Chemistry
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
1. 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.
2. 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, S. Bhattacharyya. (2011) J. Phys. Chem. B, 115, 3632-3641.
3. 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.
4. 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.
5. 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.