Tharun Sundaresan, Ph.D.

Tharun Sundaresan, Ph.D.

Name: Tharun Sundaresan, Ph.D.

USU Department of Primary Appointment: 
Biochemistry
Title: 
Associate Professor
Faculty Rank: 
Associate Professor
Location: 
Uniformed Services University of the Health Sciences, Bethesda, MD

Research Interests:
Mechanism of mRNA decay
Molecular basis of cancer

Office Phone: 
(301) 295-9423

Education

Ph.D. (Life Sciences) - Centre for Cellular and Molecular Biology (CCMB), Hyderabad, India (Affiliated to Jawaharlal Nehru University, New Delhi, India).

Representative publications, projects, and/or deployments

  • Tharun, S and Parker, R. 1995. Mechanisms of mRNA Turnover in Eukaryotic Cells. In Modern Biology Series vol:17 (mRNA metabolism and post-transcriptional gene regulation), p181-199. Ed. Harford, J.B., and Morris, D.R. John Wiley Publishers.
  • Tharun, S and Parker, R. 1999. Turnover of mRNA in eukaryotic cells. In Comprehensive natural products chemistry vol:6 (Prebiotic chemistry, molecular fossils, nucleosides and RNA), p205-216. Ed. Barton, S.D and Nakanishi, K. Pergamon Publishers.
  • Tharun, S. 2009. Lsm1-7-Pat1 complex: A link between 3’ and 5’-ends in mRNA decay? RNA Biology, 6(3):228-232.
  • Tharun, S. 2009. Roles of eukaryotic Lsm proteins in the regulation of mRNA function. International Review of Cell & Molecular Biology, 272:149-189.
  • HHMI Fellowship
  • American Cancer Society IRG grant
  • NIH RO1 Research project grant
  • USUHS Exploratory grant
  • Faculty (secondary appointment), Molecular Cell Biology Graduate Program, Uniformed Services University of the Health Sciences.
  • Course Director, Graduate Biochemistry course, Uniformed Services University of the Health Sciences.

Bibliography

  • Chowdhury, A, Swathi Kalurupalle, S and Tharun, S*. 2016. Mutagenic analysis of the C-terminal domain of Lsm1. PLoS ONE, 11: e0158876.
  • Jungfleisch, J., Chowdhury, A, Alves-Rodrigues, I, Tharun, S* and Juana Díez. 2015. The Lsm1-7-Pat1 complex promotes viral RNA translation and replication by 3 differential mechanisms. RNA, 21:1469–1479.
  • Chowdhury, A, Kalurupalle, S, and Tharun, S*. 2014. Pat1 contributes to the RNA binding activity of the Lsm1-7-Pat1 complex. RNA, 20:1465–1475.
  • Chowdhury, A, Raju, KK, Kalurupalle, S and Tharun, S*. 2012. Both Sm-domain and C-terminal extension of Lsm1 are important for the RNA-binding activity of the Lsm1–7–Pat1 complex. RNA, 18:936–944.
  • Chowdhury, A, and Tharun, S*. 2009. Activation of decapping involves binding of the mRNA and facilitation of the post-binding steps by the Lsm1-7-Pat1 complex. RNA, 15:1837–1848.
  • Tharun, S. 2008. Purification and analysis of the decapping activator Lsm1p-7p-Pat1p complex from yeast. Methods in Enzymology, 448:41-55.
  • Chowdhury, A, and Tharun, S*. 2008. lsm1 mutations impairing the ability of the Lsm1p-7p-Pat1p complex to preferentially bind to oligoadenylated RNA affect mRNA decay in vivo. RNA, 14:2149-2158.
  • Chowdhury, A, Mukhopadhyay, J. and Tharun, S*. 2007. The decapping activator Lsm1p-7p-Pat1p complex has the intrinsic ability to distinguish between oligoadenylated and polyadenylated RNAs. RNA, 13:998-1016.
  • Tharun S*, Muhlrad D, Chowdhury A and Parker R. 2005. Mutations in the Saccharomyces cerevisiae LSM1 gene that affect mRNA decapping and 3' end protection. Genetics, 170:33-46. *Corresponding author
  • Tharun, S* and Parker R. 2001. Targeting an mRNA for decapping: Displacement of translation factors and association of the Lsm1p-7p complex on deadenylated yeast mRNAs. Molecular Cell, 8:1075-1083. *Corresponding author