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| Qualifications |
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1976 B.S. University of Washington, Seattle, WA, Chemistry |
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| Research Interests |
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Our research focuses on identifying and understanding mechanisms that regulate chromatin structure and function. Currently we are studying a novel group of core histone proteins that we discovered in rat liver nucleosomes. These proteins are three times the size of conventional core histones, and have a hybrid structure consisting of a large nonhistone region and a region that closely resembles a conventional histone H2A. We call these proteins macroH2A, and currently know of three macroH2A subtypes. Recently we showed that macroH2A proteins are preferentially concentrated in the transcriptionally inactive X chromosome of female mammals. MacroH2A is also concentrated in specific chromatin domains other than the inactive X chromosome. Some of these non-X domains are composed of heterochromatin, and therefore, also appear to be transcriptionally silent. Thus, macroH2A may be involved in establishing or maintaining specific domains of transcriptionally silent chromatin. Our current projects include studies to examine macroH2A function in vivo, the effects of macroH2A on nucleosomal and higher chromatin structures, and the mechanisms involved in localizing macroH2A to specific chromosomal regions. |
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| Selected Publications |
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Pehrson, J.R. and Changolkar, L.N. Reconstitution of nucleosomes with histone macroH2A1.2. Biochemistry, 41, 179-184, 2002. Costanzi, C. and Pehrson, J.R. MacroH2A2, a new member of the macroH2A core histone family. J. Biol. Chem. 276, 21776-21784, 2001. Costanzi, C., Stein, P., Worrad, D.M., Schultz, R.M. and Pehrson, J.R. Histone macroH2A1 is concentrated in the inactive X chromosome of female preimplantation mouse embryos. Development 127, 2283-2289, 2000 Csankovszki, G., Panning, B., Bates, B., Pehrson, J.R. and Jaenisch, R. Conditional deletion of Xist disrupts histone macroH2A localization but not maintenance of X inactivation. Nature Genetics 22, 323-324, 1999. Pehrson, J.R., Litwin S., Myers, C.B. and Cohen, L.H. Pyrimidine dimer formation as a probe of nucleosome core and linker structure in situ. Methods 19, 447-456, 1999. Pehrson, J.R. and Fuji, R.N. Evolutionary conservation of histone macroH2A subtypes and domains. Nucleic Acids Res. 26, 2837-2842, 1998. Costanzi, C. and Pehrson, J.R. Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals. Nature 393: 599-601, 1998. |
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