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Identification of domains responsible for signal recognition and transduction within the QUTR transcription repressor protein

Lookup NU author(s): Dianne Smith, Dr Heather Lamb, Professor Alastair Hawkins


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QUTR (qutR-encoded transcription-repressing protein) is a multi-domain repressor protein active in the signal-transduction pathway that regulates transcription of the quinic acid utilization (qut) gene cluster in Aspergillus nidulans. In the presence of quinate, production of mRNA from the eight genes of the qut pathway is stimulated by the activator protein QUTA (qutA-encoded transcription-activating protein). Mutations in the qutR gene alter QUTR function such that the transcription of the qut gene cluster is permanently on (constitutive phenotype) or is insensitive to the presence of quinate (super-repressed phenotype). These mutant phenotypes imply that the QUTR protein plays a key role in signal recognition and transduction, and we have used deletion analysis to determine which regions of the QUTR protein are involved in these functions. We show that the QUTR protein recognizes and binds to the QUTA protein in vitro and that the N-terminal 88 amino acids of QUTR are sufficient to inactivate QUTA function in vivo. Deletion analysis and domain-swap experiments imply that the two C-terminal domains of QUTR are mainly involved in signal recognition.

Publication metadata

Author(s): Levett LJ, Si-Hoe SM, Liddle S, Wheeler K, Smith D, Lamb HK, Newton GH, Coggins JR, Hawkins AR

Publication type: Article

Publication status: Published

Journal: Biochemical Journal

Year: 2000

Volume: 350

Issue: 1

Pages: 189-197

ISSN (print): 0264-6021

ISSN (electronic): 1470-8728

Publisher: Portland Press


DOI: 10.1042/0264-6021:3500189

PubMed id: 10926843


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