This Article
Right arrow Full Text
Right arrow Full Text (PDF)
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 Wongwisansri, S.
Right arrow Articles by Laybourn, P. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Wongwisansri, S.
Right arrow Articles by Laybourn, P. J.

 Previous Article  |  Next Article 

Eukaryotic Cell, August 2005, p. 1387-1395, Vol. 4, No. 8
1535-9778/05/$08.00+0     doi:10.1128/EC.4.8.1387-1395.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Disruption of Histone Deacetylase Gene RPD3 Accelerates PHO5 Activation Kinetics through Inappropriate Pho84p Recycling

Sriwan Wongwisansri and Paul J. Laybourn*

Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, Colorado 80523-1870

Received 14 February 2005/ Accepted 20 May 2005

The histone deacetylase Rpd3p functions as a transcriptional repressor of a diverse set of genes, including PHO5. Here we describe a novel role for RPD3 in the regulation of phosphate transporter Pho84p retention in the cytoplasmic membrane. We show that under repressing conditions (with Pi), PHO5 expression is increased in a pho4{Delta} rpd3{Delta} strain, demonstrating PHO regulatory pathway independence. However, the effect of RPD3 disruption on PHO5 activation kinetics is dependent on the PHO regulatory pathway. Upon switching to activating conditions (without Pi), PHO5 transcripts accumulated more rapidly in rpd3{Delta} cells. This more rapid response correlates with a defect in phosphate uptake due to premature recycling of Pho84p, the high-affinity H+/PO43– symporter. Thus, RPD3 also participates in PHO5 regulation through a previously unidentified effect on maintenance of high-affinity phosphate uptake during phosphate starvation. We propose that Rpd3p has a negative role in the regulation of Pho84p endocytosis.

* Corresponding author. Mailing address: Department of Biochemistry and Molecular Biology, 1870 Campus Delivery, Colorado State University, Fort Collins, CO 80523-1870. Phone: (970) 491-5100. Fax: (970) 491-0494. E-mail: laybourn{at}lamar.colostate.edu.

Eukaryotic Cell, August 2005, p. 1387-1395, Vol. 4, No. 8
1535-9778/05/$08.00+0     doi:10.1128/EC.4.8.1387-1395.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Pondugula, S., Neef, D. W., Voth, W. P., Darst, R. P., Dhasarathy, A., Reynolds, M. M., Takahata, S., Stillman, D. J., Kladde, M. P. (2009). Coupling Phosphate Homeostasis to Cell Cycle-Specific Transcription: Mitotic Activation of Saccharomyces cerevisiae PHO5 by Mcm1 and Forkhead Proteins. Mol. Cell. Biol. 29: 4891-4905 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»