Open AccessCloning of the Aspergillus niger pmrA gene, a homologue of yeast PMR1 , and characterization of a pmrA null mutant
Author(s) -
Yang Jaeseung,
Kang Hyun Ah,
Ko SuMin,
Chae SuhnKee,
Ryu Dewey D.Y.,
Kim JeongYoon
Publication year - 2001
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2001.tb10657.x
Subject(s) - complementary dna , biology , mutant , aspergillus niger , yarrowia , gene , open reading frame , biochemistry , peptide sequence , nucleic acid sequence , microbiology and biotechnology
The pmrA gene, a yeast PMR1 homologue, was isolated from Aspergillus niger . Sequence analysis of the pmrA cDNA and the genomic DNA revealed that two introns exist in the coding region, and that an open reading frame in the cDNA encodes a polypeptide of 1056 amino acids containing all the conserved regions present in P‐type Ca 2+ ‐ATPases. The predicted pmrA protein exhibited a high degree of sequence similarity to the Pmr1 proteins from yeasts and mammalians (50–59% identity). The expression of the pmrA cDNA partially restored the growth defect of Yarrowia lipolytica pmr1 null mutant on EGTA‐containing medium. This indicates that the A. niger pmrA gene encodes a functional homologue of the yeast P‐type Ca 2+ ‐ATPase involved in the secretory pathway. An A. niger pmrA null mutant exhibited growth retardation on EGTA‐containing medium and the growth defect was overcome by adding Ca 2+ or Mn 2+ into the medium. This suggests an involvement of the pmrA protein in Ca 2+ and Mn 2+ homeostasis in A. niger .