This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Muro-Pastor, M. I. Articles by Scazzocchio, C. Search for Related Content PubMed PubMed Citation Articles by Muro-Pastor, M. I. Articles by Scazzocchio, C.

 Previous Article  |  Next Article 

Eukaryotic Cell, April 2004, p. 393-405, Vol. 3, No. 2
1535-9778/04/$08.00+0     DOI: 10.1128/EC.3.2.393-405.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

A Paradoxical Mutant GATA Factor

M. Isabel Muro-Pastor,^1, Joseph Strauss,² Ana Ramón,^1, and Claudio Scazzocchio^1,3*

Institut de Génétique et Microbiologie,¹ Institut Universitaire de France, Université Paris-Sud, UMR8621, 91405 Orsay Cedex, France,³ Center of Applied Genetics, University of Natural Resources and Applied Life Sciences, Vienna, Austria²

Received 27 August 2003/ Accepted 7 January 2004

The niiA (nitrite reductase) and niaD (nitrate reductase) genes of Aspergillus nidulans are subject to both induction by nitrate and repression by ammonium or glutamine. The intergenic region between these genes functions as a bidirectional promoter. In this region, nucleosomes are positioned under nonexpression conditions. On nitrate induction under derepressing conditions, total loss of positioning occurs. This is independent of transcription and of the NirA-specific transcription factor but absolutely dependent on the wide-domain GATA-binding AreA factor. We show here that a 3-amino-acid deletion in the basic carboxy-terminal sequence of the DNA-binding domain results in a protein with paradoxical properties. Its weak DNA binding is consistent with its loss-of-function phenotype on most nitrogen sources. However, it results in constitutive expression and superinducibility of niiA and niaD. Nucleosome loss of positioning is also constitutive. The mutation partially suppresses null mutations in the transcription factor NirA. AreA binds NirA in vitro, and the mutation does not affect this interaction. The in vivo methylation pattern of the promoter is drastically altered, suggesting the recruitment of one or more unknown transcription factors and/or a local distortion on the DNA double helix.

Present address: Instituto de Bioquímica Vegetal y Fotosíntesis, Centro de Investigaciones Científicas de la Isla de la Cartuja, CSIC-Universidad de Sevilla, 41092 Seville, Spain.

Present address: Sección de Bioquímica, Departamento de Biología Celular y Molecular, Facultad de Ciencias, Universidad de la República, Iguá 4225 Montevideo, Uruguay.

This article has been cited by other articles:

• Reyes-Dominguez, Y., Narendja, F., Berger, H., Gallmetzer, A., Fernandez-Martin, R., Garcia, I., Scazzocchio, C., Strauss, J. (2008). Nucleosome Positioning and Histone H3 Acetylation Are Independent Processes in the Aspergillus nidulans prnD-prnB Bidirectional Promoter. Eukaryot Cell 7: 656-663 [Abstract] [Full Text]  
• Bernreiter, A., Ramon, A., Fernandez-Martinez, J., Berger, H., Araujo-Bazan, L., Espeso, E. A., Pachlinger, R., Gallmetzer, A., Anderl, I., Scazzocchio, C., Strauss, J. (2007). Nuclear Export of the Transcription Factor NirA Is a Regulatory Checkpoint for Nitrate Induction in Aspergillus nidulans. Mol. Cell. Biol. 27: 791-802 [Abstract] [Full Text]