P. Delbecq et al., Functional analysis of the leader peptide of the yeast gene CPA1 and heterologous regulation by other fungal peptides, CURR GENET, 38(3), 2000, pp. 105-112
The 25-amino-acid leader peptide present at the 5' end of yeast CPA1 mRNA i
s responsible for the translational repression of that gene by arginine. We
show here that the active domain of the yeast peptide is highly specific a
nd extends over amino acids 6-23. The region between amino acids 6-21 is we
ll conserved between similar peptides present upstream of CPA1-homologous g
enes in other fungi. The Neurospora crassa arg-2 peptide represses the expr
ession of CPA1, whereas the peptide from Aspergillus nidulans has only a we
ak regulatory effect. Such results suggest that the N- and C-terminal amino
acids of the peptide may influence its regulatory activity. We also show t
hat the transcription start sites of CPA1 are not modified when the cells a
re grown in the presence of arginine, nor in a strain carrying an inactive
peptide.