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Scott D Briggs


  • Associate Professor of Biochemistry
HANS Room 233C

Area of Expertise:

Chromatin and histone modifications: In the eukaryotic cell, the precise organization and regulation of chromatin is critical for many cellular processes such as transcription, replication, recombination, repair, and chromosomal segregation. Although chromatin is defined as DNA associated with proteins, the fundamental repeating unit of chromatin is the nucleosome. The nucleosome consists of two copies of each core histone protein (H3, H4, H2A, and H2B) and 146 base pairs of DNA that wraps twice around them. Histone proteins contain a central histone-fold domain and N- and C-terminal tail domains that are subjected to extensive posttransitional modifications. Since posttransitional modifications on histones such as acetylation, phosphorylation, ubiquitination, and/or methylation can influence the chromatin environment and ultimately gene expression, we are interested in studying the enzymes and their associated proteins that mediate these modifications and how misregulation of these enzymes can lead to a disease state.

Histone methyltransferases and Cancer: Many SET domain-containing proteins have been associated with human cancers suggesting that they play an important regulatory roll in the cell. However, only a few have been identified as histone methyltransferases such as MLL1 and EZH2. Many of these SET domain-containing proteins are found either mutated, chromosomal translocated, or over-expressed when isolated from oncogenic cells. Therefore, we are interested in determining how mis-regulation and/or aberrant expression of these methyltransferases can lead to an oncogenic event and how aberrant histone methylation may play a role in oncogenesis. 

Awards & Honors

(2012) Kohls Outstanding Undergraduate Teacher Award for Biochemistry. Purdue University Department of Biochemistry.

(2011) Faculty Scholar. Purdue University.

(2010) Faculty Scholar. Purdue University.

(2006) Seed for Success. Purdue University.

(2004) Fellowship. Leukemia and Lymphoma Society.

(2004) Sidney Kimmel Scholar. Sidney Kimmel Foundation.

(2004) Walther Assistant Professor of Biochemistry. Walther Cancer Institute.


Briggs, S. D. Patent on the development of a histone methyl-specific antibody that recognizes histone H4 that is methylated at Arg3.

Selected Publications

Harmeyer, K., South, P., Bishop, B., Ogas, J., & Briggs, S. (2014). Immediate chromatin immunoprecipitation and on-bead quantitative PCR analysis: a versatile and rapid ChIP procedure. Nucleic Acids Res, pii: gku1347. Retrieved from

South, P., Harmeyer, K., Serratore, N., & Briggs, S. (2013). H3K4 methyltransferase Set1 is involved in maintenance of ergosterol homeostasis and resistance to Brefeldin A. Proc. Natl. Acad. Sci. U.S.A, 11, E1016-E1025. Retrieved from

Mersman, D., Du, H., Fingerman, I., & South, S. (2012). Charge-based interaction conserved within hisone H3 lysine 4 (H3K4) methyltransferase complexes is needed for protein stability, histone methylation, and gene expression. J. Biol. Chem, 287, 2652-2665. Retrieved from

South, P. (2011). ASH2L (ash2 (absent, small, or homeotic)-like (Drosophila)) Atlas of Genetics and Cytogenetics in Oncology and Haematology, N/A. Retrieved from

Mersman, D., Du, H., Fingerman, I., & South, P. (2011). Charge-based Interaction Conserved within Histone H3 Lysine 4 (H3K4) Methyltransferase Complexes is needed for Protien Stability, Histone Methylation, and Gene Expression. Journal of Biological Chemistry, 287(4), 2652-2665.

South, P. (2011). Understanding the Structure and Function of ASH2L. Atlas of Genetics and Cytogenetics in Oncology and Haematology, N/A. Retrieved from

South, P., Fingerman, I., Mersman, D., & Du, H. (2010). A conserved interaction between the SDI domain of Bre2 and the Dpy-3- Domain of Sdc1 is required for histone methylation and gene expression. J. Biol. Chem, 285(1), 595-607. Retrieved from

Du, H. (2010). A nucleosome surface formed by histone H4, H2A, and H3 residues is needed for proper histone H3 Lys36 methylation, histone acetylation, and repression of cryptic transcription. J. Biol. Chem, 285, 11704-11713. Retrieved from

Dhawan, R., Luo, H., Foerster, A., AbuQamar, S., Du, H., Briggs, S., . . . Mengiste, T. (2009). HISTONE MONOUBIQUITINATION 1 interacts with a subunit of the mediator complex and regulates defense responses against necrotrophic fungal pathogens. Plant Cell, 21, 1000-1019.