Document Detail

Conserved Ser/Arg-rich motif in PPZ orthologs from fungi is important for its role in cation tolerance.
MedLine Citation:
PMID:  22232558     Owner:  NLM     Status:  MEDLINE    
PPZ1 orthologs, novel members of a phosphoprotein phosphatase family of phosphatases, are found only in fungi. They regulate diverse physiological processes in fungi e.g. ion homeostasis, cell size, cell integrity, etc. Although they are an important determinant of salt tolerance in fungi, their physiological role remained unexplored in any halotolerant species. In this context we report here molecular and functional characterization of DhPPZ1 from Debaryomyces hansenii, which is one of the most halotolerant and osmotolerant species of yeast. Our results showed that DhPPZ1 knock-out strain displayed higher tolerance to toxic cations, and unlike in Saccharomyces cerevisiae, Na(+)/H(+) antiporter appeared to have an important role in this process. Besides salt tolerance, DhPPZ1 also had role in cell wall integrity and growth in D. hansenii. We have also identified a short, serine-arginine-rich sequence motif in DhPpz1p that is essential for its role in salt tolerance but not in other physiological processes. Taken together, these results underscore a distinct role of DhPpz1p in D. hansenii and illustrate an example of how organisms utilize the same molecular tool box differently to garner adaptive fitness for their respective ecological niches.
Anupriya Minhas; Anupam Sharma; Harsimran Kaur; Yashpal Rawal; Kaliannan Ganesan; Alok K Mondal
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2012-01-09
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  287     ISSN:  1083-351X     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2012 Mar 
Date Detail:
Created Date:  2012-03-05     Completed Date:  2012-04-24     Revised Date:  2013-06-26    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  7301-12     Citation Subset:  IM    
Institute of Microbial Technology, Council of Scientific and Industrial Research, Sector 39A, Chandigarh 160 036, India.
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MeSH Terms
Amino Acid Motifs
Debaromyces / enzymology*,  genetics*
Gene Knockdown Techniques
Osmotic Pressure
Phosphoprotein Phosphatases / genetics*,  metabolism*
Saccharomyces cerevisiae / enzymology*,  genetics*
Saccharomyces cerevisiae Proteins / genetics*,  metabolism*
Sequence Homology, Amino Acid
Reg. No./Substance:
0/Cations; 0/Saccharomyces cerevisiae Proteins; EC protein, S cerevisiae; EC Phosphatases

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