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Protein phosphatase Z (Ppz) is a fungus specific enzyme that regulates cell wall integrity, cation homeostasis and oxidative stress response. Work on  Saccharomyces cerevisiae  has shown that the enzyme is inhibited by Hal3/Vhs3 moonlighting proteins that together with Cab3 constitute the essential phosphopantothenoylcysteine decarboxylase (PPCDC) enzyme. In  Candida albicans  CaPpz1 is also involved in the morphological changes and infectiveness of this opportunistic human pathogen. To reveal the CaPpz1 regulatory context we searched the  C .  albicans  database and identified two genes that, based on the structure of their  S .  cerevisiae  counterparts, were termed CaHal3 and CaCab3. By pull down analysis and phosphatase assays we demonstrated that both of the bacterially expressed recombinant proteins were able to bind and inhibit CaPpz1 as well as its C-terminal catalytic domain (CaPpz1-Cter) with comparable efficiency. The binding and inhibition were always more pronounced with CaPpz1-Cter, indicating a protective effect against inhibition by the N-terminal domain in the full length protein. The functions of the  C .  albicans  proteins were tested by their overexpression in  S .  cerevisiae . Contrary to expectations we found that only CaCab3 and not CaHal3 rescued the phenotypic traits that are related to phosphatase inhibition by ScHal3, such as tolerance to LiCl or hygromycin B, requirement for external K +  concentrations, or growth in a MAP kinase deficient  slt2  background. On the other hand, both of the  Candida  proteins turned out to be essential PPCDC components and behaved as their  S .  cerevisiae  counterparts: expression of CaCab3 and CaHal3 rescued the  cab3  and  hal3 vhs3 S .  cerevisiae  mutations, respectively. Thus, both CaHal3 and CaCab3 retained the PPCDC related functions and have the potential for CaPpz1 inhibition  in vitro . The fact that only CaCab3 exhibits its phosphatase regulatory potential  in vivo  suggests that in  C .  albicans  CaCab3, but not CaHal3, acts as a moonlighting protein.

plos one

Analysis of Two Putative Candida albicans Phosphopantothenoylcysteine Decarboxylase / Protein Phosphatase Z Regulatory Subunits Reveals an Unexpected Distribution of Functional Roles