Letter abstract
Nature Cell Biology 10, 707 - 715 (2008)
Published online: 18 May 2008 | doi:10.1038/ncb1733
Yeast Ataxin-7 links histone deubiquitination with gene gating and mRNA export
Alwin Köhler1,2, Maren Schneider1, Ghislain G. Cabal3, Ulf Nehrbass3 & Ed Hurt1
Targeting of a gene to the nuclear pore complexes (NPCs), known as gene gating, can affect its transcriptional state1, 2, 3, 4, 5, 6, 7, 8, 9. However, the mechanism underlying gene gating is poorly understood. Here, we have identified SAGA-associated Sgf73 (ref. 10), the yeast orthologue of human Ataxin-7 (ref. 11), as a regulator of histone H2B ubiquitin levels, a modification linked to both transcription initiation and elongation12, 13. Sgf73 is a key component of a minimal histone-deubiquitinating complex. Activation of the H2B deubiquitinating protease, Ubp8, is cooperative and requires complex formation with the amino-terminal zinc-finger-containing domain of Sgf73 and Sgf11–Sus1. Through a separate domain, Sgf73 mediates recruitment of the TREX-2 mRNA export factors Sac3 and Thp1 to SAGA and their stable interaction with Sus1–Cdc31. This latter step is crucial to target TREX-2 to the NPC. Loss of Sgf73 from SAGA abrogates gene gating of GAL1 and causes a GAL1 mRNA export defect. Thus, Sgf73 provides a molecular scaffold to integrate the regulation of H2B ubiquitin levels, tethering of a gene to the NPC and export of mRNA.
- Biochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, 69120 Heidelberg, Germany.
- Universitätskinderklinik Heidelberg, Im Neuenheimer Feld 151, 69120 Heidelberg, Germany.
- Unité de Biologie Cellulaire du Noyau, Institut Pasteur, 25 rue du Dr Roux, 75724 Paris cedex 15, France.
Correspondence to: Ed Hurt1 e-mail: ed.hurt@bzh.uni-heidelberg.de
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