Assistant Professor, Ph.D.
Lab Location: 330 SEB
Lab Phone: (248) 370-4905
(248) 370-4225 FAX
Degree: Ph.D., National Institute of Immunology, India 2001
- BIO 325, Biochemistry I
- BIO 511, Advanced Topics (Cellular, Biochem lab)
- BIO Bio Communications - II
- Principal Investigator: 1R01GM095514-01A1 08/01/2011 - 07/31/2016)
- National Institutes of Health
Regulation of Chromatin Structure During Transcription.
The packaging of eukaryotic DNA into nucleosomes, the basic unit of chromatin, plays a central role in regulating all DNA dependent processes. Nucleosomes are composed of DNA wrapped around an octamer of histone proteins– H3, H4, H2A and H2B. We are interested in understanding the molecular mechanisms that govern the dynamic alterations of chromatin structure during transcription. Several multi-protein complexes, including histone modifying and ATP-dependent chromatin remodeling complexes, are utilized by cells to alter or even remove nucleosomes to facilitate transcription. The current focus of our research is on understanding the importance of co-transcriptional histone acetylation in modulating chromatin plasticity during RNA polymerase elongation. We recently showed that hyperacetylated histones are evicted from coding sequences during RNA polymerase elongation. Through the use of yeast genetics in the model organism Saccharomyces cerevisiae, biochemistry and molecular biology techniques, we are investigating whether acetylation dependent histone eviction is mediated by the recruitment and function of RSC, an essential chromatin remodeling complex known to bind acetylated histones and to remodel chromatin by evicting histones.
Govind, C.K., Ginsburg, D., and Hinnebusch, A.G. (2012). Measuring Dynamic Changes in Histone Modifications and Nucleosome Density during Activated Transcription in Budding Yeast. Methods in Molecular Biololgy 833, 15-27.
Spain, M.M., and Govind, C.K. (2011). A role for phosphorylated Pol II CTD in modulating transcription coupled histone dynamics. Transcription 2, 78-81.
Govind, C.K., Qiu, H., Ginsburg, D.S., Ruan, C., Hofmeyer, K., Hu, C., Swaminathan, V., Workman, J.L., Li, B., and Hinnebusch, A.G. (2010). Phosphorylated Pol II CTD Recruits Multiple HDACs, Including Rpd3C(S), for Methylation-Dependent Deacetylation of ORF Nucleosomes. Molecular Cell 39, 234-246.
Ginsburg, D.S., Govind, C.K., and Hinnebusch, A.G. (2009). NuA4 Lysine Acetyltransferase Esa1 Is Targeted to Coding Regions and Stimulates Transcription Elongation with Gcn5. Molecular and Cellular Biology 29, 6473-6487.
Pascual-Garcia, P., Govind, C.K., Queralt, E., Cuenca-Bono, B., Llopis, A., Chavez, S., Hinnebusch, A.G., and Rodriguez-Navarro, S. (2008). Sus1 is recruited to coding regions and functions during transcription elongation in association with SAGA and TREX2. Genes & Development 22, 2811-2822.
Govind, C.K., Zhang, F., Qiu, H., Hofmeyer, K., and Hinnebusch, A.G. (2007). Gcn5 promotes acetylation, eviction, and methylation of nucleosomes in transcribed coding regions. Molecular Cell 25, 31-42. (Selected as a Must Read by Faculty of 1000)
Acharya, K.K., Govind, C.K., Shore, A.N., Stoler, M.H., and Reddi, P.P. (2006). cis-Requirement for the maintenance of round spermatid-specific transcription. Developmental Biology 295, 781-790. (Selected as a Recommended Read by Faculty of 1000)
Govind, C.K., Yoon, S., Qiu, H., Govind, S., and Hinnebusch, A.G. (2005). Simultaneous recruitment of coactivators by Gcn4p stimulates multiple steps of transcription in vivo. Molecular and Cellular Biology 25, 5626-5638. (Selected as a Recommended Read by Faculty of 1000)
Kim, S.J., Swanson, M.J., Qiu, H., Govind, C.K., and Hinnebusch, A.G. (2005). Activator Gcn4p and Cyc8p/Tup1p are interdependent for promoter occupancy at ARG1 in vivo. Molecular and Cellular Biology 25, 11171-11183. (Selected as a Recommended Read by Faculty of 1000)
Yoon, S., Govind, C.K., Qiu, H., Kim, S.J., Dong, J., and Hinnebusch, A.G. (2004). Recruitment of the ArgR/Mcm1p repressor is stimulated by the activator Gcn4p: a self-checking activation mechanism. Proc Natl Acad Sci (PNAS) U S A 101, 11713-11718.