microbiology, Vol 142, 1477-1490, Copyright © 1996 by Society for General Microbiology

ARTICLES

The QUTA activator and QUTR repressor proteins of Aspergillus nidulans interact to regulate transcription of the quinate utilization pathway genese [published erratum appears in Microbiology 1996 Oct;142(Pt 10):2983]

HK Lamb, GH Newton, LJ Levett, E Cairns, CF Roberts and AR Hawkins
Department of Biochemistry and Genetics, Medical School, University of Newcastle, Newcastle upon Tyne, UK.

Genetic evidence suggests that the activity of the native QUTA transcription activator protein is negated by the action of the QUTR transcription repressor protein. When Aspergillus nidulans was transformed with plasmids containing the wild-type qutA gene, transformants that constitutively expressed the quinate pathway enzymes were isolated. The constitutive phenotype of these transformants was associated with an increased copy number of the transforming qutA gene and elevated qutA mRNA levels. Conversely, when A. nidulans was transformed with plasmids containing the qutR gene under the control of the constitutive pgk promoter, transformants with a super-repressed phenotype (unable to utilize quinate as a carbon source) were isolated. The super-repressed phenotype of these transformants was associated with an increased copy number of the transforming qutR gene and elevated qutR mRNA levels. These copy-number-dependent phenotypes argue that the levels of the QUTA and QUTR proteins were elevated in the high- copy-number transformants. When diploid strains were formed by combining haploid strains that contained high copy numbers of either the qutA gene (constitutive phenotype) or the qutR gene (super- repressing; non-inducible phenotype), the resulting diploid phenotype was one of quinate-inducible production of the quinate pathway enzymes, in a manner similar to wild-type. The simplest interpretation of these observations is that the QUTR repressor protein mediates its repressing activity through a direct interaction with the QUTA activator protein. Other possible interpretations are discussed in the text. Experiments in which truncated versions of the QUTA protein were produced in the presence of a wild-type QUTA protein indicate that the QUTR repressor protein recognizes and binds to the C-terminal half of the QUTA activator protein.

This article has been cited by other articles:

				H. K. Lamb, J. Ren, A. Park, C. Johnson, K. Leslie, S. Cocklin, P. Thompson, C. Mee, A. Cooper, D. K. Stammers, et al. Modulation of the ligand binding properties of the transcription repressor NmrA by GATA-containing DNA and site-directed mutagenesis Protein Sci., December 1, 2004; 13(12): 3127 - 3138. [Abstract] [Full Text] [PDF]

				H. K. Lamb, K. Leslie, A. L. Dodds, M. Nutley, A. Cooper, C. Johnson, P. Thompson, D. K. Stammers, and A. R. Hawkins The Negative Transcriptional Regulator NmrA Discriminates between Oxidized and Reduced Dinucleotides J. Biol. Chem., August 22, 2003; 278(34): 32107 - 32114. [Abstract] [Full Text] [PDF]