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Daniel S. Och University Professor of Cell and Developmental Biology Ph.D., 1987, University of Michigan 1051 BRB II/III/6058
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Our research focuses on regulation of the nuclear genome in mammals and model organisms. The long strands of nuclear DNA are associated with packaging proteins, called histones, into a structure known as chromatin, akin to the way thread is organized around a spool. We are particularly interested in changes in this chromatin structure via chemical modification of the histone proteins, and how attachment of certain chemical groups onto the histones leads to altered chromatin function. These targeted structural changes are conceptually like the unraveling of the thread to reach specific, buried sections. We are also fascinated by functional changes in chromatin, caused by these histone modifications, that persist through cell division from one cell into two daughter cells; these persistent, or epigenetic, changes are of particular interest because they are key to normal and abnormal growth: they occur during organismal development into multicellular tissues and organs, and are typically disrupted during abnormal reversal of tissue specialization and growth control as in cancer, as well as during aging of cells and individuals. Selected Publications: Dang, W, Steffers KK, Perry R, Dorsey JA, Johnson FB, Shilatifard A, Kaeberlein M, Kennedy BK, Berger SL. (2009) Histone H4 lysine 16 acetylation regulates cellular lifespan. Nature (in press) Berger SL, Kouzarides T, Shiekhattar R, Shilatifard A. (2009) An operational definition of epigenetics. Genes & Development 23:781-783. Lin YY, Lu, JY, Zhang J, Walter W, Dang W, Wan J, Tao SC, Qian J, Zhao Y, Boeke JD, Berger SL, Zhu H. (2009) Protein acetylation microarray reveal NuA4 controls key metabolic target regulating gluconeogenesis. Cell 136:1073-1084. Berger SL. (2008) Out of the jaws of death: Prmt5 steers p53. Nature Cell Biology 10:1389-1390. Zediak V and Berger SL. (2008) Hit and Run: Transient activation of deubiquitylase activity in a chromatin remodeling complex. Molecular Cell 31:773-774. Walter W, Clynes D, Tang Y, Marmorstein R, Mellor J, Berger SL. (2008) 14-3-3 interaction with histone H3 involves dual modification pattern of phosphoacetylation. Molecular and Cellular Biology 28:2840-2849. Huang J and Berger SL. (2008) The emerging field of lysine methylation of non-histone proteins. Current Opinion in Genetics 18:152-158. Huang J, Sengupta R, Espejo A, Lee MG, Dorsey JA, Richter M, Opravil S, Shiekhattar R, Bedford MT, Jenuwein T, and Berger SL. (2007) p53 is regulated by the lysine demethylase LSD1. Nature 449:105-108. |
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