Glucose repression of transcription of the Schizosaccharomyces pombe fbp1 gene occurs by a cAMP signaling pathway

• Published in: Genes & development Vol. 5; no. 4; pp. 561 - 571
• Main Authors: Hoffman, C S, Winston, F
• Format: Journal Article
• Language: English
• Published: Cold Spring Harbor, NY Cold Spring Harbor Laboratory 01.04.1991
• Subjects: Biological and medical sciences; Cloning, Molecular; Cyclic AMP - physiology; Fructose-Bisphosphatase - genetics; Fundamental and applied biological sciences. Psychology; Genes, Fungal - drug effects; Genes, Suppressor; Genotype; Glucose - pharmacology; Molecular and cellular biology; Molecular genetics; Restriction Mapping; Schizosaccharomyces - drug effects; Schizosaccharomyces - enzymology; Schizosaccharomyces - genetics; Schizosaccharomyces pombe; Signal Transduction; Transcription, Genetic - drug effects; Transcription. Transcription factor. Splicing. Rna processing; Fructose-bisphosphatase; Yeast; Transcription; Enzyme; Cyclic AMP; Glucose; Repression; Fungi; Northern blotting; Adenylate cyclase; Regulation(control); Protein kinase; Schizosaccharomyces pombe; Ascomycetes; Mechanism of action; Thallophyta
• ISSN: 0890-9369; 1549-5477
• DOI: 10.1101/gad.5.4.561

Transcription of the fbp1 gene, encoding fructose-1,6-bisphosphatase, of Schizosaccharomyces pombe is subject to glucose repression. Previous work has demonstrated that several genes (git genes) are required for this repression. In this report we demonstrate that one of these genes, git2, is the same as the cyr1 gene, which encodes adenylate cyclase, and that loss-of-function mutations in git2 cause constitutive fbp1 transcription. Addition of cAMP to the growth medium suppresses the transcriptional defect in git2 mutants as well as in strains that carry mutations in any of six additional git genes. Similarly, exogenous cAMP represses fbp1 transcription in wild-type cells grown on a derepressing carbon source. Different levels of adenylate cyclase activity in different git2 mutants, coupled with the result that some git2 mutants display intragenic complementation, strongly suggest that adenylate cyclase acts as a multimer and that different git2 mutations alter distinct activities of adenylate cyclase, including catalytic activity and response to glucose. Additional experiments demonstrate that this cAMP signaling pathway is independent of the S. pombe ras1 gene and works by activation of cAMP-dependent protein kinase.