Mark R. Parthun PhD
Mark R. Parthun PhD
357A Hamilton Hall 1645 Neil Avenue Columbus OH 43210
- Experimental Therapeutics
General Research InterestAssembly and regulation of chromatin structure
Research Description My research program focuses on understanding the role of histone post-translational modifications in the formation and regulation of chromatin structure. Chromatin is the nucleoprotein structure that enables chromosomal DNA to be condensed and packaged in eukaryotic nuclei. Chromatin structure plays an active role in the regulation of many cellular processes that involve accessing chromosomal DNA, such as transcription, DNA replication, recombination and DNA repair. The primary protein components of chromatin are the core histones (H2A, H2B, H3, and H4). A fundamental mechanism for controlling chromatin structure is through the post-translational modification of the core histones. The primary emphasis of the research in my laboratory is in characterizing type B histone acetyltransferases (HATs). Histone acetyltransferases, which can be broadly divided into two categories, type A and type B, are responsible for the acetylation of lysine residues in the core histones. Type B HATs are responsible for the acetylation of newly synthesized histones H3 and H4 that occurs in conjunction with the process of chromatin assembly. We are taking both biochemical and molecular genetic approaches toward understanding the function of these enzymes using models organisms such as S. cerevisiae.
Transinstitutional WorkWe are actively involved in collaborations with other members of the Ohio State University comprehensive Cancer Center. Working with Dr. John Byrd, Dr. Michael Freitas, Dr. Michael Grever and Dr. Guido Marcucci we have been working to characterize the complement of histone proteins present in the cells of leukemia patients to determine the role of chromatin structure in the development and progression of leukemia. In addition, we are working to understand the changes in histone proteins that occur in patients that are treated with agents in clinical trials that target histone post-translational modifications.
Sandhu SK, Volinia S, Costinean S, Galasso M, Neinast R, Santhanam R, Parthun MR, Perrotti D, Marcucci G, Garzon R, Croce CMmiR-155 targets histone deacetylase 4 (HDAC4) and impairs transcriptional activity of B-cell lymphoma 6 (BCL6) in the Eμ-miR-155 transgenic mouse model.Proc Natl Acad Sci U S A 109(49) 20047-52 12/4/2012
Parthun MRHistone acetyltransferase 1: More than just an enzyme?Biochim Biophys Acta 1819(3-4) 256-63 3/1/2012
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