Functional analysis of the leader peptide of the yeast gene CPA1 and heterologous regulation by other fungal peptides

• Published in: Current genetics Vol. 38; no. 3; pp. 105 - 112
• Main Authors: Delbecq, P, Calvo, O, Filipkowski, R K, Piérard, A, Messenguy, F
• Format: Journal Article
• Language: English
• Published: United States 04.10.2000
• Subjects: Amino Acid Sequence; Aspergillus nidulans; Aspergillus nidulans - genetics; Base Sequence; Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing); CPA1 gene; DNA, Fungal - genetics; DNA, Fungal - isolation & purification; Fungal Proteins - biosynthesis; Fungal Proteins - genetics; Gene Expression Regulation, Fungal - physiology; Genes, Fungal - physiology; Molecular Sequence Data; Neurospora crassa; Neurospora crassa - genetics; Protein Biosynthesis; Protein Sorting Signals - genetics; RNA, Fungal - biosynthesis; RNA, Fungal - genetics; RNA, Messenger - biosynthesis; RNA, Messenger - genetics; Saccharomyces cerevisiae; Saccharomyces cerevisiae - drug effects; Saccharomyces cerevisiae - genetics; Saccharomyces cerevisiae Proteins; Sequence Deletion; Sequence Homology, Amino Acid; Transcription, Genetic
• ISSN: 0172-8083; 1432-0983
• DOI: 10.1007/s002940000140

The 25-amino-acid leader peptide present at the 5' end of yeast CPA1 mRNA is responsible for the translational repression of that gene by arginine. We show here that the active domain of the yeast peptide is highly specific and extends over amino acids 6-23. The region between amino acids 6-21 is well conserved between similar peptides present upstream of CPA1-homologous genes in other fungi. The Neurospora crassa arg-2 peptide represses the expression of CPA1, whereas the peptide from Aspergillus nidulans has only a weak regulatory effect. Such results suggest that the N- and C-terminal amino acids of the peptide may influence its regulatory activity. We also show that the transcription start sites of CPA1 are not modified when the cells are grown in the presence of arginine, nor in a strain carrying an inactive peptide.