HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 276, Issue 31, 28659-28666, August 3, 2001

This Article Full Text Full Text (PDF) All Versions of this Article: 276/31/28659    most recent M102280200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by van der Merwe, G. K. Articles by van Vuuren, H. J. J. Search for Related Content PubMed PubMed Citation Articles by van der Merwe, G. K. Articles by van Vuuren, H. J. J.

Ammonia Regulates VID30 Expression and Vid30p Function Shifts Nitrogen Metabolism toward Glutamate Formation Especially when Saccharomyces cerevisiae Is Grown in Low Concentrations of Ammonia^*

George K. van der Merwe, Terrance G. Cooper^§, and Hennie J. J. van Vuuren^¶

From the  Wine Research Center, Faculty of Agricultural Sciences, University of British Columbia, Vancouver, British Columbia V6T 1Z4, Canada and the ^§ Department of Microbiology and Immunology, University of Tennessee, Memphis, Tennessee 38163

The GATA family proteins Gln3p and Gat1p mediate nitrogen catabolite repression (NCR)-sensitive transcription in Saccharomyces cerevisiae. When cells are cultured with a good nitrogen source (glutamine, ammonia), Gln3p and Gat1p are restricted to the cytoplasm, whereas with a poor nitrogen source (proline), they localize to the nucleus, bind to the GATA sequences of NCR-sensitive gene promoters, and activate transcription. The target of rapamycin-signaling cascade and Ure2p participate in regulating the cellular localization of Gln3p and Gat1p. Rapamycin, a Tor protein inhibitor, like growth with a poor nitrogen source, promotes nuclear localization of Gln3p and Gat1p. gln3 and ure2 mutants are partially resistant and hypersensitive to growth inhibition by rapamycin, respectively. We show that a vid30 is more rapamycin-sensitive than wild type but less so than a ure2. VID30 expression is modestly NCR-sensitive, responsive to deletion of URE2, and greatly increases in low ammonia medium. Patterns of gene expression in a vid30 suggest that the Vid30p function shifts the balance of nitrogen metabolism toward the production of glutamate, especially when cells are grown in low ammonia. CAN1, DAL4, DAL5, MEP2, DAL1, DAL80, and GDH3 transcription is down-regulated by Vid30p function with proline as the nitrogen source. An effect, however, that could easily be indirect.

This article has been cited by other articles:

				H. Cai, M. Hauser, F. Naider, and J. M. Becker Differential Regulation and Substrate Preferences in Two Peptide Transporters of Saccharomyces cerevisiae Eukaryot. Cell, October 1, 2007; 6(10): 1805 - 1813. [Abstract] [Full Text] [PDF]

				J. C. Panepinto, B. G. Oliver, J. R. Fortwendel, D. L. H. Smith, D. S. Askew, and J. C. Rhodes Deletion of the Aspergillus fumigatus Gene Encoding the Ras-Related Protein RhbA Reduces Virulence in a Model of Invasive Pulmonary Aspergillosis Infect. Immun., May 1, 2003; 71(5): 2819 - 2826. [Abstract] [Full Text] [PDF]

				J. Regelmann, T. Schule, F. S. Josupeit, J. Horak, M. Rose, K.-D. Entian, M. Thumm, and D. H. Wolf Catabolite Degradation of Fructose-1,6-bisphosphatase in the Yeast Saccharomyces cerevisiae: A Genome-wide Screen Identifies Eight Novel GID Genes and Indicates the Existence of Two Degradation Pathways Mol. Biol. Cell, April 1, 2003; 14(4): 1652 - 1663. [Abstract] [Full Text] [PDF]