This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental material
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Koues, O. I.
Right arrow Articles by Greer, S. F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Koues, O. I.
Right arrow Articles by Greer, S. F.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, October 2008, p. 5837-5850, Vol. 28, No. 19
0270-7306/08/$08.00+0     doi:10.1128/MCB.00535-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Regulation of Acetylation at the Major Histocompatibility Complex Class II Proximal Promoter by the 19S Proteasomal ATPase Sug1{triangledown} ,{dagger}

Olivia I. Koues,1 R. Kyle Dudley,2 Agnieszka D. Truax,2 Dawson Gerhardt,1 Kavita P. Bhat,2 Sam McNeal,2 and Susanna F. Greer2*

Division of Molecular Genetics and Biochemistry,1 Division of Cellular and Molecular Biology and Physiology, Department of Biology, Georgia State University, Atlanta, Georgia 303022

Received 2 April 2008/ Returned for modification 20 May 2008/ Accepted 7 July 2008

Recent studies have made evident the fact that the 19S regulatory component of the proteasome has functions that extend beyond degradation, particularly in the regulation of transcription. Although 19S ATPases facilitate chromatin remodeling and acetylation events in yeast (Saccharomyces cerevisiae), it is unclear if they play similar roles in mammalian cells. We have recently shown that the 19S ATPase Sug1 positively regulates the transcription of the critical inflammatory gene for major histocompatibility complex class II (MHC-II) by stabilizing enhanceosome assembly at the proximal promoter. We now show that Sug1 is crucial for regulating histone H3 acetylation at the MHC-II proximal promoter. Sug1 binds to acetylated histone H3 and, in the absence of Sug1, histone H3 acetylation is dramatically decreased at the proximal promoter, with a preferential loss of acetylation at H3 lysine 18. Sug1 also binds to the MHC-II histone acetyltransferase CREB-binding protein (CBP) and is critical for the recruitment of CBP to the MHC-II proximal promoter. Our current study strongly implicates the 19S ATPase Sug1 in modifying histones to initiate MHC-II transcription and provides novel insights into the role of the proteasome in the regulation of mammalian transcription.


* Corresponding author. Mailing address: Department of Biology, College of Arts and Sciences, P.O. Box 4010, Atlanta, GA 30302-4010. Phone: (404) 413-5403. Fax: (404) 413-5301. E-mail: sgreer{at}gsu.edu

{triangledown} Published ahead of print on 28 July 2008.

{dagger} Supplemental material for this article may be found at http://mcb.asm.org/.


Molecular and Cellular Biology, October 2008, p. 5837-5850, Vol. 28, No. 19
0270-7306/08/$08.00+0     doi:10.1128/MCB.00535-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Middeldorp, J., Kamphuis, W., Sluijs, J. A., Achoui, D., Leenaars, C. H. C., Feenstra, M. G. P., van Tijn, P., Fischer, D. F., Berkers, C., Ovaa, H., Quinlan, R. A., Hol, E. M. (2009). Intermediate filament transcription in astrocytes is repressed by proteasome inhibition. FASEB J. 23: 2710-2726 [Abstract] [Full Text]  
  • Ferry, C., Gianni, M., Lalevee, S., Bruck, N., Plassat, J.-L., Raska, I. Jr., Garattini, E., Rochette-Egly, C. (2009). SUG-1 Plays Proteolytic and Non-proteolytic Roles in the Control of Retinoic Acid Target Genes via Its Interaction with SRC-3. J. Biol. Chem. 284: 8127-8135 [Abstract] [Full Text]