title: SAGA and a novel Drosophila export complex anchor efficient transcription and mRNA export to NPC.
abstract: SAGA/TFTC-type multiprotein complexes play important roles in the regulation of transcription. We have investigated the importance of the nuclear positioning of a gene, its transcription and the consequent export of the nascent mRNA. We show that E(y)2 is a subunit of the SAGA/TFTC-type histone acetyl transferase complex in Drosophila and that E(y)2 concentrates at the nuclear periphery. We demonstrate an interaction between E(y)2 and the nuclear pore complex (NPC) and show that SAGA/TFTC also contacts the NPC at the nuclear periphery. E(y)2 forms also a complex with X-linked male sterile 2 (Xmas-2) to regulate mRNA transport both in normal conditions and after heat shock. Importantly, E(y)2 and Xmas-2 knockdown decreases the contact between the heat-shock protein 70 (hsp70) gene loci and the nuclear envelope before and after activation and interferes with transcription. Thus, E(y)2 and Xmas-2 together with SAGA/TFTC function in the anchoring of a subset of transcription sites to the NPCs to achieve efficient transcription and mRNA export.
authors.affiliation: Department of Regulation of Gene Expression, Institute of Gene Biology, Russian Academy of Sciences, Moscow, Russia.
authors.forename: Maria M
authors.initials: MM
authors.lastname: Kurshakova
authors.forename: Alexey N
authors.initials: AN
authors.lastname: Krasnov
authors.forename: Daria V
authors.initials: DV
authors.lastname: Kopytova
authors.forename: Yulii V
authors.initials: YV
authors.lastname: Shidlovskii
authors.forename: Julia V
authors.initials: JV
authors.lastname: Nikolenko
authors.forename: Elena N
authors.initials: EN
authors.lastname: Nabirochkina
authors.forename: Danièle
authors.initials: D
authors.lastname: Spehner
authors.forename: Patrick
authors.initials: P
authors.lastname: Schultz
authors.forename: Làszlò
authors.initials: L
authors.lastname: Tora
authors.forename: Sofia G
authors.initials: SG
authors.lastname: Georgieva
mesh_terms: D000818:Animals; D002460:Cell Line; D002467:Cell Nucleus / Q000378:metabolism; D002875:Chromosomes / Q000378:metabolism; D020285:Cryoelectron Microscopy; D029721:Drosophila Proteins / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D004331:Drosophila melanogaster / Q000235:genetics / Q000378:metabolism*; D005786:Gene Expression Regulation; D018840:HSP70 Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism; D006801:Humans; D007150:Immunohistochemistry; D008297:Male; D046912:Multiprotein Complexes / Q000737:chemistry / Q000378:metabolism*; D009685:Nuclear Envelope / Q000378:metabolism; D022022:Nuclear Pore / Q000378:metabolism*; D021122:Protein Subunits / Q000235:genetics / Q000378:metabolism; D034622:RNA Interference; D034443:RNA Transport / Q000502:physiology*; D012333:RNA, Messenger / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000235:genetics / Q000378:metabolism; D014157:Transcription Factors / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D014158:Transcription, Genetic; D020798:Two-Hybrid System Techniques
chemical_list: D029721:Drosophila Proteins; D018840:HSP70 Heat-Shock Proteins; D046912:Multiprotein Complexes; D021122:Protein Subunits; D012333:RNA, Messenger; D016601:RNA-Binding Proteins; D014157:Transcription Factors; C423782:e(y)2 protein, Drosophila; C527103:xmas protein, Drosophila