Anita Nag
Visiting Assistant Professor of Biology and Chemistry
- Email: anita.nag@furman.edu
- Phone: 864.294.2354
- Office: Plyler 244D, Townes Science Center
Anita Nag grew up in Calcutta, India. She received her B.Sc. in Chemistry from Jadavpur University, India, and M.Sc. in Chemistry from Indian Institute of Technology, in Kanpur. She moved to California and completed her Ph.D. in Chemistry with emphasis on Biochemistry from University of California, Los Angeles. At UCLA, she worked with Professor Harold Martinson to study functional coupling among various stages of messenger RNA processing. After receiving her Ph.D., she joined the laboratory of Professor Joan Steitz at Yale University where she worked on RNA decay factors. Dr. Nag received the Anna Fuller Postdoctoral Fellowship and Leukemia Lymphoma Postdoctoral Fellowship to conduct her postdoctoral research. She was intrigued by the functional diversity of virally encoded RNAs and joined the laboratory of Professor Hengli Tang at Florida State University where she worked with the Hepatitis C virus.
Dr. Nag served as Assistant Professor at Florida A&M University before joining Furman. She collaborated in multiple projects, trained several undergraduate students, and actively developed new courses implementing modern pedagogical approach.
Dr. Nag received awards including ASM-LINK Undergraduate Faculty Research Initiative (UFRI) fellowship by American Society of Microbiology, and funding from Research Center in Minority Institution (NIMHD). Dr. Nag enjoys mentoring undergraduate students in her research laboratory. At Furman, she continues her research on viral RNAs.
Education
- Ph.D.,University of California, Los Angeles
- M.Sc., Indian Institute of Technology, Kanpur
- B.Sc., Jadavpur University
Research
My research group is interested in understanding various functional RNAs encoded by different viruses. Viruses cause dampening of gene expression through selective inhibition of host protein translation, and by destabilizing the host messenger RNA. Several viruses including Kaposi’s sarcoma virus, SARS corona virus encode viral proteins that actively engage with the ribosome on mRNA. However, some viral RNAs may escape this RNA destabilization step. We are particularly interested in understanding how viral RNAs escape these destabilization steps in the host cell. We use biochemical and molecular biology techniques to study viral RNA and protein complexes that are involved in this host shut-off pathway.
Publications
- Herbert, K.; Nag, A. A Tale of Two RNAs during Viral Infection: How Viruses Antagonize mRNAs and Small Non-Coding RNAs in The Host Cell. Viruses 2016, 8 (6), 154.
- Nag, A.; Robotham, J. M.; Tang, H. Suppression of Viral RNA Binding and the Assembly of Infectious Hepatitis C Virus Particles in Vitro by Cyclophilin Inhibitors. J. Virol. 2012, 86 (23), 12616-12624.
- Nag, A.; Steitz, J. A. Tri-snRNP-Associated Proteins Interact with Subunits of the TRAMP and Nuclear Exosome Complexes, Linking RNA Decay and Pre-mRNA Splicing. RNA Biol. 2012, 9 (3), 334-342.
- Tsao, D. C.; Park, N. J.; Nag, A.; Martinson, H. G. Prolonged α-Amanitin Treatment of Cells for Studying Mutated Polymerases Causes Degradation of DSIF160 and Other Proteins. RNA 2012, 18(2), 222-229.
- Yang, F.; Robotham, J. M.; Grise, H.; Frausto, S.; Madan, V.; Zayas, M.; Bartenschlager, R.; Robinson, M.; Greenstein, A. E.; Nag, A.; et al. A Major Determinant of Cyclophilin Dependence and Cyclosporine Susceptibility of Hepatitis C Virus Identified by a Genetic Approach. PLoS Pathog. 2010, 6 (9), e1001118.
- Nag, A.; Narsinh, K.; Martinson, H. G. The poly(A)-Dependent Transcriptional Pause Is Mediated by CPSF Acting on the Body of the Polymerase. Nat. Struct. Mol. Biol. 2007, 14 (7), 662-669.
- Nag, A.; Narsinh, K.; Kazerouninia, A.; Martinson, H. G. The Conserved AAUAAA Hexamer of the poly(A) Signal Can Act Alone to Trigger a Stable Decrease in RNA Polymerase II Transcription Velocity. RNA 2006, 12 (8), 1534-1544.
- Rigo, F.; Kazerouninia, A.; Nag, A.; Martinson, H. G. The RNA Tether from the Poly(A) Signal to the Polymerase Mediates Coupling of Transcription to Cleavage and Polyadenylation. Mol. Cell 2005, 20(5), 733-745.
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