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Biochemistry Faculty

Venkat Gopalan


Dr. Gopalan
Associate Professor

Phone:  614-292-1332
Fax:      614-292-6773
email:  gopalan.5@osu.edu
Webpage: Gopalan Homepage
 



Research Interests:

Structure and mechanism of action of ribonuclease P, a catalytic ribonucleoprotein (RNP) complex. The endoribonuclease RNase P is a ubiquitous RNP that is involved in the maturation of tRNAs. In Escherichia coli, the RNase P holoenzyme consists of a catalytic RNA subunit (M1 RNA, 377 nts) and a protein cofactor (C5 protein, 119 amino acid residues). The long-term goal of our studies is to elucidate the mechanism of assembly of this unique catalytic RNP complex and thereby understand how an RNA-binding protein influences the structure and function of its RNA ligand. 2. Use of plant RNase P to inhibit gene expression Recently, it has been demonstrated that endogenous, cellular RNase P can be guided to specifically destroy a target mRNA in bacterial and human cells in tissue culture. Our aim is to determine if plant RNase P could be utilized to disrupt gene expression in plants and their pathogens. These studies will help establish plant RNase P as a valuable functional genomics tool. Towards this objective, we have recently made significant progress in partially purifying and characterizing plant RNase P.



Selected publications from the last 5 years:

Gopalan, V.. (2007) "Uniformity amid diversity in RNase P." Proc Natl Acad Sci U S A. 104(7), 2031-2.

Tsai HY, Pulukkunat DK, Woznick WK, Gopalan, V.. (2006) "Functional reconstitution and characterization of Pyrococcus furiosus RNase P." Proc Natl Acad Sci U S A. 103(44), 16147-52.

Rangarajan S, Raj ML, Hernandez JM, Grotewold E, Gopalan V.  (2004) "RNase P as a tool for disruption of gene expression in maize cells.", Biochem J. 380(Pt 3), 611-6.

Pulukkunat DK, Raj ML, Pattanayak D, Lai LB, Gopalan V. (2003) "Exploring the potential of plant RNase P as a functional genomics tool.". Methods Mol Biol. 236, 295-310.

Boomershine, W.P., Stephen Raj, M.L., Gopalan V., and Foster, M.P. (2003) "Preparation of uniformly labeled NMR samples in Escherichia coli under the tight control of the araBAD promoter: expression of an archaeal homolog of the RNase P Rpp29 protein." Protein Expr Purif. 28, 246-51.

Tsai, H.Y., Masquida, B., Biswas, R., Westhof, E., and Gopalan V. (2003) "Molecular modeling of the three-dimensional structure of the bacterial RNase P holoenzyme." J Mol Biol. 325, 661-75.

Jovanovic, M., Sanchez, R., Altman, S., and Gopalan V. (2002) "Elucidation of structure-function relationships in the protein subunit of bacterial RNase P using a genetic complementation approach." Nucleic Acids Res.30, 5065-73.

Guerrier-Takada, C., Eder, P.S., Gopalan V., and Altman, S. (2002) "Purification and characterization of Rpp25, an RNA-binding protein subunit of human ribonuclease P." RNA 8, 290-5.

Tsai, H.Y., Lai, L.B., and Gopalan V. (2002) "A Modified pBluescript-based vector for facile cloning and transcription of RNAs." Anal Biochem.303, 214-7.

Eubank, T.D., Biswas, R., Jovanovic, M., Litovchick, A., Lapidot, A., and Gopalan V. (2002) "Inhibition of bacterial RNase P by aminoglycoside-arginine conjugates." FEBS Lett. 511, 107-12.

Gopalan, V., Vioque, A., and Altman, S. (2002) "RNase P: variations and uses." J Biol Chem. 277, 6759-62.

Stephen Raj, M. L., Pulukkunat, D. K., Reckard, J. F., Thomas, G. and Gopalan V.  (2001.)  "Cleavage of bipartite substrates by rice and maize RNase P: Application to targeted degradation of mRNAs in plants." Plant Physiology 125: 1187-1190.

Biswas, R., Kuhne, H., Brudvig, G. and Gopalan V.  (2001) "Use of EPR spectroscopy to study macromolecular function." Science Progress 84: 45-68.

Wu, C-W., Eder, P.S., Gopalan V. and Behrman, E. J. (2001).   "Kinetics of coupling reactions that generate monothiophosphate disulfides Implications for modification of RNAs." Bioconjugate Chemistry 12: 842-844.

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The Ohio State University - Department of Biochemistry
776 Biological Sciences Building, 484 West 12th Avenue
Columbus, Ohio 43210
TEL: 614.292.6771
FAX: 614.292.6773
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