fission yeast gene (prr1+) that encodes a response regulator implicated in oxidative stress response

• Published in: Journal of biochemistry (Tokyo) Vol. 125; no. 6; pp. 1061 - 1066
• Main Authors: Ohmiya, R, Kato, C, Yamada, H, Aiba, H, Mizuno, T
• Format: Journal Article
• Language: English
• Published: England Oxford University Press 01.06.1999
• Subjects: Aspartic Acid - metabolism; cold; DNA-Binding Proteins - genetics; DNA-Binding Proteins - metabolism; exons; Fungal Proteins - genetics; Fungal Proteins - metabolism; Gene Expression Regulation, Fungal; Genes, Fungal; genetic regulation; His-Asp phosphorelay; Histidine - metabolism; hydrogen peroxide; introns; messenger RNA; Mitogen-Activated Protein Kinases - metabolism; Models, Biological; Molecular Sequence Data; mutants; oxidation; Oxidative Stress; Phenotype; potassium chloride; regulator genes; response regulator; Schizosaccharomyces - genetics; Schizosaccharomyces - growth & development; Schizosaccharomyces - metabolism; Schizosaccharomyces pombe; Schizosaccharomyces pombe Proteins; Signal Transduction; stress; stress response; transcription (genetics); Transcription Factors - genetics; Transcription Factors - metabolism
• ISSN: 0021-924X; 1756-2651
• DOI: 10.1093/oxfordjournals.jbchem.a022387

An inspection of the Schizosaccharomyces pombe genome database revealed that this eukaryotic microorganism possesses a gene that may encode a bacterial type of histidine-to-aspartate (His-Asp) phosphorelay component, namely, a response regulator. The predicted gene, named prrl+ (S.pombe response regulator), encodes a protein that contains a typical phospho-accepting receiver domain, preceded by a mammalian heat shock factor (HSF)-like DNA-binding domain. Inactivation of this prrl+ gene resulted in mutant cells defective in some aspects of stress responses, including sensitivity to oxidative stress, cold-temperature, and heavy metal toxicity. It was also demonstrated that Prrl is required for the transcription of some genes {e.g., trrl+, cttl+), which are induced by oxidative stress. These results suggest that a His-Asp phosphorelay system may be involved in a stress-activated signaling pathway in S. pombe.