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Lysine Methylation and Regulation of Gene Expression Programs
Author(s) -
Gozani Or
Publication year - 2012
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.26.1_supplement.467.2
Subject(s) - histone methyltransferase , epigenetics , histone code , chromatin , histone , histone methylation , biology , epigenomics , computational biology , chromatin remodeling , histone h3 , genetics , microbiology and biotechnology , dna methylation , gene expression , gene , nucleosome
My laboratory is interested in understanding the molecular mechanisms by which chromatin signaling networks effect nuclear and epigenetic programs, and how disruption in these mechanisms contribute to cancer and other pathologic states. Our work centers on the biology of protein lysine methylation, a principal chromatin‐regulatory mechanism thought to be involved in directing epigenetic processes. We study how lysine methylation events on histone and non‐histone nuclear factors are generated, sensed, and transduced, and how these chemical marks integrate with other modification and nuclear signaling systems to govern diverse functions. We previously demonstrated that the PHD finger ( P lant H omeo d omain), a signature chromatin‐associated domain, functions as a novel recognition module for histone H3 trimethylated at lysine 4. We linked this single histone species to multiple different functions via its recognition by discrete PHD finger nuclear proteins, including providing evidence that disrupting the read‐out of a histone modification can cause an inherited human disease. I will discuss new work focusing on an expression library containing the majority of predicted protein lysine methyltransferase (PKMT) enzymes present in the human genome, and studies aimed at elucidating the role of PKMTs in oncogenic programming. I will also present recent work employing protein microarray technologies for discovery and biological characterization of new methyllysine‐binding domains and methylation events.