title: Functional characterization of the Drosophila Hmt4-20/Suv4-20 histone methyltransferase.
abstract: Di- and trimethylation of histone H4 lysine20 (H4K20) are thought to play an important role in controlling gene expression in vertebrates and in Drosophila. By inducing a null mutation in Drosophila Suv4-20, we show that it encodes the histone H4 lysine20 di- and trimethyltransferase. In Suv4-20 mutants, the H4K20 di- and trimethyl marks are strongly reduced or absent, and the monomethyl mark is significantly increased. We find that even with this biochemical function, Suv4-20 is not required for survival and does not control position-effect variegation (PEV).
authors.affiliation: Department of Molecular Biology and Biochemistry, Waksman Institute, New Jersey Cancer Center, Rutgers University, Piscataway, NJ 08854-8020, USA.
authors.forename: Ayako
authors.initials: A
authors.lastname: Sakaguchi
authors.forename: Dmitry
authors.initials: D
authors.lastname: Karachentsev
authors.forename: Mansha
authors.initials: M
authors.lastname: Seth-Pasricha
authors.forename: Marina
authors.initials: M
authors.lastname: Druzhinina
authors.forename: Ruth
authors.initials: R
authors.lastname: Steward
mesh_terms: D000818:Animals; D015153:Blotting, Western; D029721:Drosophila Proteins / Q000235:genetics*; D004331:Drosophila melanogaster / Q000201:enzymology*; D011495:Histone-Lysine N-Methyltransferase / Q000235:genetics*; D009154:Mutation / Q000235:genetics; D020133:Reverse Transcriptase Polymerase Chain Reaction
chemical_list: D029721:Drosophila Proteins; C487546:Hmt4-20 protein, Drosophila; D011495:Histone-Lysine N-Methyltransferase