Brian D. Strahl

UNC Professor of Biochemistry & Biophysics

Brian Strahl is a chromatin biologist located at the University of North Carolina (UNC) School of Medicine.  His research aims to decipher how histone post-translational modifications regulate the diverse functions associate with DNA in the context of chromatin. 

Histone Modifications and the Histone Code

The Strahl lab is focused on understanding how a class of proteins called histones compacts our genetic information (DNA) and how these proteins contribute to the regulation of functions associated with DNA (gene regulation, DNA replication and DNA repair for example).  Histones are post-translational modified with a wide number of chemical modifications or "tags" (such as acetylation, methylation, and phosphorylation).  How they all contribute to chromatin (DNA/Histone) organization and function is not well understood, but many studies suggest they work in the form of a ‘histone code’ to regulate these events.  Brian Strahl’s lab is working on understanding how histone modifications functions (singly and in combination) using a number of distinct platforms (proteomics, etc.) and model systems (yeast and humans). 

The Strahl lab is located at UNC Chapel Hill

Recent Publications:


Cornett, E. M., Dickson, B. M., Vaughan, R. M., Trievel, R. C., Strahl, B. D. & Rothbart, S. B. Substrate specificity profiling of histone-modifying enzymes by peptide microarray. Methods in Enzymology. (In Press).

Sorenson, M. R., Jha, D. K., Ucles, S., Flood, D., Strahl, B. D., Stevens, S. W. & Kress, T. L. (2016) Histone H3K36 methylation regulates pre-mRNA splicing in Saccharomyces cerevisiae. RNA Biology(In Press).

Hattori, T., Lai, D., Dementieva, I. S., Montano, S. P., Zheng, Y., Akin, L., Swift, K., M., Grzybowski, A. T., Koide, A., Krajewski, K., Strahl, B. D., Kelleher, N. L., Ruthenburg, A. J. & Koide, S. (2016) Antigen clasping by two antigen-binding sites of an exceptionally specific antibody for histone methylation. Proc Natl Acad Sci USA (In Press).

Andrews, F. H.*, Shanle, E. K.*, Strahl, B. D.* & Kutateladze, T. G.* (2016) Acetyllysine binding activity of the YEATS domains is essential for transcription. Transcription (In Press).

Andrews, F. H., Gatchalian, J., Krajewski, K., Strahl, B. D. & Kutateladze, T. G. (2016) Regulation of methyllysine readers through phosphorylation. ACS Chemical Biology. DOI: 10.1021/acschembio.5b00802.


Cliffe, A. R., Vogel, J. L., Arbuckle, J. H., Geden, M. J., Rothbart, S. B., Cusack, C. L., Strahl, B. D., Kristie, T. M., Deshmukh, M. A (2015) Neuronal stress pathway mediating a histone Methyl/Phospho switch is required for Herpes Simplex Virus Reactivation. Cell Host and Microbe. 18:649-658

Shanle, E. K., Tsun, I. K. & Strahl, B. D. (2015) A course-based undergraduate research experience investigating p300 bromodomain mutations. Biochemistry and Molecular Biology Education. doi: 10.1002/bmb.20927.

Chen, S., Ze, Y., Wilkinson, A., Deshpande, A. J., Krajewski, K., Strahl, B. D., Armstrong, S. A., Patel, D., J. & Gozani, O. (2105) The PZP domain of AF10 senses unmodified H3K27 to regulate DOT1L-mediated methylation of H3K79. Molecular Cell.

Shanle, E. K, Andrews, F. H., Meriesh, H., McDaniel, S. L., Dronamraiu, R., DiFiore J., Jha, D., Wozniak, G. G., Bridgers, J., Kerschner, J. L., Martin, G. M., Morrison A. J., Krajewski, K., Kutateladze, T*. & Strahl, B. D.* (2015) Association of Taf14 with acetylated histone H3 directs gene transcription and the DNA damage response. Genes & Development. 29:1789-1794.

Simon, J. M., Parker, J. S., Liu, F., Rothbart, S. B., Ait-Si-Ali, S., Strahl, B. D., Jin, j., Davis, I. J., Mosley, A. L. & Pattenden, P. G. (2015) A role for Widely Interspaced Zinc finger (WIZ) in retention of the G9a methyltransferase on chromatin. Journal of Biological Chemistry. 290:26088-26102.

Zhang, Z.-M., Rothbart, S. B., Allison, D., Cai, Q., Harrison, J. S., Li, L., Wang, Y., Strahl B. D., Wang, G. G., Song, J. (2015) An allosteric interaction links USP7 to deubiquitination and chromatin targeting of UHRF1. Cell Reports. 12:1400-1406.

Ali, F. A., Daze, K. D., Rothbart, S. B., Strongin, D. E., Rincon-Arano, H., Allen, H. F., Li, J., Groudine, M., Strahl, B. D., Hof, F. & Kutateladze, T. G. (2015) Calixarenes selectively inhibit binding of the PHD fingers to histone H3K4me3. Journal of Biological Chemistry. 290:22919-22930.

Rothbart, S. B., Dickson, B. M., Raab, J. R., Grzybowski, A. T., Krajewski, K., Guo, A. H., Shanle, E. K., Josefowicz, S. Z., Fuchs, S. M., Allis, C. D., Magnuson, T. R., Ruthenburg, A. J. & Strahl, B. D.(2015) An interactive database for the assessment of histone antibody specificity. Molecular Cell. 59:502-511.

Wang, L., Xie, L., Ramachandran, S., Lee, Y., Yan, Z., Zhou, L., Krajewski, K., Liu, F., Zhu, C., Chen, D., Strahl, B. D., Jin, J., Dokholyan, N. V. & Chen, X. (2015) Non-canonical bromodomain within DNA-PKcs promotes DNA damage response and radioresistance through recognizing an IR-induced acetyl-lysine on H2AX. Chemistry & Biology. 22:1-13.

Rothbart, S. B.*, Dickson, B. M. & Strahl, B. D.* (2015) From Histones to Ribosomes: A Chromatin Regulator Tangoes with Translation. In Press at Cancer Discovery. 5:228-230.

Perfetti, M. T., Baughman, B. M., Dickson, B. D. Mu, Y., Cui, G., Mader, P., Dong, A., Norris, J. L., Rothbart, S. B., Strahl, B. D., Brown, P. J., Janzen, W. P., Arrowsmith, C. H., Mer, G., McBride, K., James, L., & Frye, S. V. (2015) Identification of a Fragment-like Small Molecule Ligand for the Methyl-lysine Binding Protein, 53BP1. ACS Chemical Biology. 10:1072-1081.

McKay, D. J., Klusza, S., Penke, T. J., R., Meers, M. P., Curry, K. P., McDaniel, S. L., Malek, P. Y., Cooper, S. W., Tatomer, D., C., Lieb, J. D., Strahl, B. D., Duronio, R. J. & Matera, A. G. (2015) Interrogating the function of metazoan histones using engineered gene clusters. Developmental Cell. 32:373-86.

Tong, Q., Mazur, S., J., Rincon-Arona, H., Rothbart, S. B., Kuznetsov, D. M., Cui, G., Liu, W. H., Gete, Y., Klein, B. J., Jenkins, L., Mer, G., Kutatelasze, A., G., Strahl, B. D., Groudine, M., G., Appella, E. & Kutateladze, T., G. (2015) An acetyl-methyl switch drives a conformational change in p53. Structure. 23:322-31.

Tong, Q., Cui, G., Botuyan, M. V., Rothbart, S. B., Hayashi, R., Musselman, C. A., Appella, E., Strahl, B. D., Mer, G. & Kutateladze, T. G. (2015) Structural plasticity of methyllysine recognition by the tandem Tudor domain of 53BP1. Structure. 23:312-21.

Dumesic, P. A., Homer, C. M., Moresco, J. J., Pack, L. R., Shanle, E. K., Coyle, S. M., Strahl, B. D., Fujimori, D. G., Yates, J. R. & Madhani, H. D. (2015) Product binding enforces the genomic specificity of a yeast polycomb repressive complex. Cell. 160:1-15.

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