![[Feedback]](/icons/banner/feedbackACT.gif){kind=icon}
![[For Subscribers]](/icons/banner/subscriberACT.gif){kind=icon}
![[Archive]](/icons/banner/archiveACT.gif){kind=icon}
![[Search]](/icons/banner/searchACT.gif){kind=icon}
|
|
|
|
|
||
A more recent version of this article appeared on October 1, 2006
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Submitted on February 3, 2006
Revised on June 20, 2006
Accepted on July 11, 2006
*Biochemie-Zentrum der Universität Heidelberg, INF328, D-69120, Heidelberg, Germany; University Children’s Hospital Heidelberg, INF150, D-69120, Heidelberg, Germany; Centro de Investigación Príncipe Felipe, E-46013, Valencia, Spain; ||Cell Signaling Unit, Departament de Ciencies Experimentals i de la Salut, Universitat Pompeu Fabra, E-08003, Barcelona, Spain
Monitoring Editor: Susan Wente
Sus1 acts in nuclear mRNA export via its association with the nuclear pore-associated Sac3-Thp1-Cdc31 complex. In addition, Sus1 plays a role in transcription through its interaction with the SAGA complex. Here, we have analyzed function and interaction of Sus1 within the SAGA complex. We demonstrate that Sus1 is involved in the SAGA-dependent histone H2B deubiquitinylation and maintenance of normal H3 methylation levels. By deletion analyses we show that binding of Sus1 to SAGA depends on the deubiquitinylating enzyme Ubp8 and Sgf11. Moreover, a stable subcomplex between Sus1, Sgf11 and Ubp8 could be dissociated from SAGA under high salt conditions. In vivo recruitment of Sus1 to the activated GAL1 promoter depends on Ubp8 and vice versa. In addition, histones coenrich during SAGA purification in a Sus1-Sgf11-Ubp8 dependent way. Interestingly, sgf11 deletion enhances the mRNA export defect observed in sus1
cells. Thus, the Sus1-Sgf11-Ubp8 module could work at the junction between SAGA-dependent transcription and nuclear mRNA export.
These authors contributed equally to this work.
Address correspondence to:
Susana Rodríguez-Navarro (srodriguez{at}cipf.es)
This article has been cited by other articles:
|
|
 |
|
  P. Pascual-Garcia, C. K. Govind, E. Queralt, B. Cuenca-Bono, A. Llopis, S. Chavez, A. G. Hinnebusch, and S. Rodriguez-Navarro Sus1 is recruited to coding regions and functions during transcription elongation in association with SAGA and TREX2 Genes & Dev., October 15, 2008; 22(20): 2811 - 2822. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 C. Gonzalez-Aguilera, C. Tous, B. Gomez-Gonzalez, P. Huertas, R. Luna, and A. Aguilera The THP1-SAC3-SUS1-CDC31 Complex Works in Transcription Elongation-mRNA Export Preventing RNA-mediated Genome Instability Mol. Biol. Cell, October 1, 2008; 19(10): 4310 - 4318. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. E. Grund, T. Fischer, G. G. Cabal, O. Antunez, J. E. Perez-Ortin, and E. Hurt The inner nuclear membrane protein Src1 associates with subtelomeric genes and alters their regulated gene expression J. Cell Biol., September 8, 2008; 182(5): 897 - 910. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 L. Chen and K. Madura Centrin/Cdc31 Is a Novel Regulator of Protein Degradation Mol. Cell. Biol., March 1, 2008; 28(5): 1829 - 1840. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. A. Chekanova, K. C. Abruzzi, M. Rosbash, and D. A. Belostotsky Sus1, Sac3, and Thp1 mediate post-transcriptional tethering of active genes to the nuclear rim as well as to non-nascent mRNP RNA, January 1, 2008; 14(1): 66 - 77. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 L. Laprade, D. Rose, and F. Winston Characterization of New Spt3 and TATA-Binding Protein Mutants of Saccharomyces cerevisiae: Spt3 TBP Allele-Specific Interactions and Bypass of Spt8 Genetics, December 1, 2007; 177(4): 2007 - 2017. [Abstract] [Full Text] [PDF]
|
|
