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Conserved Ser/Arg-rich motif in PPZ orthologs from fungi is important for its role in cation tolerance.

DIR@IMTECH: CSIR-Institute of Microbial Technology

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Title Conserved Ser/Arg-rich motif in PPZ orthologs from fungi is important for its role in cation tolerance.
 
Creator Minhas, Anupriya
Sharma, Anupam
Kaur, Harsimran
Rawal, Yashpal
Ganesan, K
Mondal, Alok K
 
Subject QR Microbiology
 
Description 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.
 
Publisher American Society for Biochemistry and Molecular Biology
 
Date 2012-03-02
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://crdd.osdd.net/open/1271/1/mondal2012.pdf
Minhas, Anupriya and Sharma, Anupam and Kaur, Harsimran and Rawal, Yashpal and Ganesan, K and Mondal, Alok K (2012) Conserved Ser/Arg-rich motif in PPZ orthologs from fungi is important for its role in cation tolerance. The Journal of biological chemistry, 287 (10). pp. 7301-12. ISSN 1083-351X
 
Relation http://www.jbc.org/content/287/10/7301.long
http://crdd.osdd.net/open/1271/