| Autor: |
Yang, Jaeseung, Kang, Hyun Ah, Ko, Su‐Min, Chae, Suhn‐Kee, Ryu, Dewey D.Y., Kim, Jeong‐Yoon |
| Zdroj: |
FEMS Microbiology Letters; May 2001, Vol. 199 Issue: 1 p97-102, 6p |
| Abstrakt: |
The pmrAgene, a yeast PMR1homologue, was isolated from Aspergillus niger. Sequence analysis of the pmrAcDNA 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 Ca2+‐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 pmrAcDNA partially restored the growth defect of Yarrowia lipolytica pmr1null mutant on EGTA‐containing medium. This indicates that the A. niger pmrAgene encodes a functional homologue of the yeast P‐type Ca2+‐ATPase involved in the secretory pathway. An A. niger pmrAnull mutant exhibited growth retardation on EGTA‐containing medium and the growth defect was overcome by adding Ca2+or Mn2+into the medium. This suggests an involvement of the pmrA protein in Ca2+and Mn2+homeostasis in A. niger. |
| Databáze: |
Supplemental Index |
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