title: The RNA helicase Rm62 cooperates with SU(VAR)3-9 to re-silence active transcription in Drosophila melanogaster.
abstract: Gene expression is highly dynamic and many genes show a wide range in expression over several orders of magnitude. This regulation is often mediated by sequence specific transcription factors. In addition, the tight packaging of DNA into chromatin can provide an additional layer of control resulting in a dynamic range of gene expression covering several orders of magnitude. During transcriptional activation, chromatin barriers have to be eliminated to allow an efficient progression of the RNA polymerase. This repressive chromatin structure has to be re-established quickly after it has been activated in order to tightly regulate gene activity. We show that the DExD/H box containing RNA helicase Rm62 is targeted to a site of rapid induction of transcription where it is responsible for an increased degree of methylation at H3K9 at the heat shock locus after removal of the heat shock stimulus. The RNA helicase interacts with the well-characterized histone methyltransferase SU(VAR)3-9 via its N-terminus, which provides a potential mechanism for the targeting of H3K9 methylation to highly regulated genes. The recruitment of SU(VAR)3-9 through interaction with a RNA helicase to a site of active transcription might be a general mechanism that allows an efficient silencing of highly regulated genes thereby enabling a cell to fine tune its gene activity over a wide range.
authors.affiliation: Munich Center of Integrated Protein Science and Adolf-Butenandt Institute, Ludwig Maximilians University of Munich, Munich, Germany.
authors.forename: Joern
authors.initials: J
authors.lastname: Boeke
authors.forename: Indira
authors.initials: I
authors.lastname: Bag
authors.forename: M Janaki
authors.initials: MJ
authors.lastname: Ramaiah
authors.forename: Irene
authors.initials: I
authors.lastname: Vetter
authors.forename: Elisabeth
authors.initials: E
authors.lastname: Kremmer
authors.forename: Manika
authors.initials: M
authors.lastname: Pal-Bhadra
authors.forename: Utpal
authors.initials: U
authors.lastname: Bhadra
authors.forename: Axel
authors.initials: A
authors.lastname: Imhof
mesh_terms: D000818:Animals; D004331:Drosophila melanogaster / Q000201:enzymology* / Q000235:genetics* / Q000378:metabolism; D018840:HSP70 Heat-Shock Proteins / Q000172:deficiency / Q000235:genetics; D006657:Histones / Q000737:chemistry / Q000378:metabolism; D008239:Lysine / Q000378:metabolism; D008745:Methylation; D008780:Methyltransferases / Q000378:metabolism*; D011485:Protein Binding; D020365:RNA Helicases / Q000378:metabolism*; D034622:RNA Interference; D014158:Transcription, Genetic / Q000235:genetics*
chemical_list: D018840:HSP70 Heat-Shock Proteins; D006657:Histones; D008780:Methyltransferases; C445404:SU(VAR)3-9; D020365:RNA Helicases; D008239:Lysine