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Candida albicans CaPTC6 is a functional homologue for Saccharomyces cerevisiae ScPTC6 and encodes a type 2C protein phosphatase
Author(s) -
Yu Liquan,
Zhao Jingwen,
Feng Jinrong,
Fang Jiaping,
Feng Chen,
Jiang Yuanying,
Cao Yongbing,
Jiang Linghuo
Publication year - 2010
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/yea.1743
Subject(s) - biology , saccharomyces cerevisiae , candida albicans , yeast , phosphatase , biochemistry , enzyme , gene , fungal protein , mitochondrion , microbiology and biotechnology
Type 2C protein phosphatases (PP2C) are monomeric enzymes and their activities require the presence of magnesium or manganese ions. There are seven PP2C genes, ScPTC1, ScPTC2, ScPTC3, ScPTC4, ScPTC5, ScPTC6 and ScPTC7 , in Saccharomyces cerevisiae . PTC6 is highly conserved in pathogenic and nonpathogenic yeasts. In the current study we have demonstrated that the Candida albicans CaPTC6 gene could complement the functions of ScPTC6 in the rapamycin and caffeine sensitivities of S. cerevisiae cells, indicating that they are functional homologues. We have also demonstrated that the CaPTC6 ‐encoded protein is a typical PP2C enzyme and that CaPtc6p is localized in the mitochondrion of yeast‐form and hyphal cells. However, deletion of CaPTC6 neither affects cell and hyphal growth nor renders Candida cells sensitive to rapamycin and caffeine. Therefore, possibly with a functional redundancy to other mitochondrial phosphatases, CaPtc6p is likely to be involved in the regulation of a mitochondrial physiology. Copyright © 2009 John Wiley & Sons, Ltd.