Document Detail


Novel acid phosphatase in Candida glabrata suggests selective pressure and niche specialization in the phosphate signal transduction pathway.
MedLine Citation:
PMID:  20739710     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Evolution through natural selection suggests unnecessary genes are lost. We observed that the yeast Candida glabrata lost the gene encoding a phosphate-repressible acid phosphatase (PHO5) present in many yeasts including Saccharomyces cerevisiae. However, C. glabrata still had phosphate starvation-inducible phosphatase activity. Screening a C. glabrata genomic library, we identified CgPMU2, a member of a three-gene family that contains a phosphomutase-like domain. This small-scale gene duplication event could allow for sub- or neofunctionalization. On the basis of phylogenetic and biochemical characterizations, CgPMU2 has neofunctionalized to become a broad range, phosphate starvation-regulated acid phosphatase, which functionally replaces PHO5 in this pathogenic yeast. We determined that CgPmu2, unlike ScPho5, is not able to hydrolyze phytic acid (inositol hexakisphosphate). Phytic acid is present in fruits and seeds where S. cerevisiae grows, but is not abundant in mammalian tissues where C. glabrata grows. We demonstrated that C. glabrata is limited from an environment where phytic acid is the only source of phosphate. Our work suggests that during evolutionary time, the selection for the ancestral PHO5 was lost and that C. glabrata neofunctionalized a weak phosphatase to replace PHO5. Convergent evolution of a phosphate starvation-inducible acid phosphatase in C. glabrata relative to most yeast species provides an example of how small changes in signal transduction pathways can mediate genetic isolation and uncovers a potential speciation gene.
Authors:
Brianne R Orkwis; Danielle L Davies; Christine L Kerwin; Dominique Sanglard; Dennis D Wykoff
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2010-08-25
Journal Detail:
Title:  Genetics     Volume:  186     ISSN:  1943-2631     ISO Abbreviation:  Genetics     Publication Date:  2010 Nov 
Date Detail:
Created Date:  2010-11-10     Completed Date:  2011-02-15     Revised Date:  2013-05-28    
Medline Journal Info:
Nlm Unique ID:  0374636     Medline TA:  Genetics     Country:  United States    
Other Details:
Languages:  eng     Pagination:  885-95     Citation Subset:  IM    
Affiliation:
Department of Biology, Villanova University, Villanova, Pennsylvania 19085, USA.
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MeSH Terms
Descriptor/Qualifier:
Acid Phosphatase / biosynthesis,  chemistry,  metabolism*
Amino Acid Sequence
Candida glabrata / drug effects,  enzymology*,  genetics*,  growth & development
Enzyme Induction / drug effects
Evolution, Molecular
Fungal Proteins / chemistry,  genetics,  metabolism
Gene Expression Regulation, Fungal / drug effects
Gene Library
Genes, Fungal / genetics
Genetic Complementation Test
Hydrolysis / drug effects
Molecular Sequence Data
Mutation / genetics
Open Reading Frames / genetics
Phosphates / deficiency,  metabolism*,  pharmacology
Recombinant Fusion Proteins / metabolism
Selection, Genetic*
Sequence Alignment
Signal Transduction* / drug effects
Substrate Specificity / drug effects
Chemical
Reg. No./Substance:
0/Fungal Proteins; 0/Phosphates; 0/Recombinant Fusion Proteins; EC 3.1.3.2/Acid Phosphatase
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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