Loss of Dfg5 glycosylphosphatidylinositol‐anchored membrane protein confers enhanced heat tolerance in Saccharomyces cerevisiae. (7th January 2015)

• Record Type: Journal Article
• Authors: Nasution, Olviyani; Lee, Jaok; Srinivasa, Kavitha; Choi, In‐Geol; Lee, Young Mi; Kim, Eunjung; Choi, Wonja; Kim, Wankee
• Is Part Of: Environmental microbiology. Volume 17:Number 8(2015:Aug.)
• Page Start: 2721
• Page End: 2734
• Publication Date: 2015-01-07
• Subjects: Microbial ecology -- Periodicals; Environmental Microbiology -- Periodicals; 579.17
• DOI: 10.1111/1462-2920.12649
• Languages: English
• ISSNs: 1462-2912

Abstract

<abstract abstract-type="main"> <title>Summary</title> <p>The protein product of <italic>S</italic><italic>accharomyces cerevisiae</italic> <italic>DFG</italic><italic>5</italic> gene is a glycosylphosphatidylinositol (GPI)‐anchored plasma membrane protein and a putative glycosidase/glycosyltransferase that links other GPI‐anchored proteins to β‐glucans in the cell wall. Upon exposure to heat (41°C), <italic>DFG</italic><italic>5</italic> deletion mutant <italic>dfg5</italic>Δ displayed significantly enhanced heat tolerance as well as lowered level of reactive oxygen species and decreased membrane permeability compared with those in the control (BY4741). Comparative transcriptome profiles of BY4741 and <italic>dfg5</italic>Δ revealed that 38 and 23 genes were up‐ and down‐regulated in <italic>dfg5</italic>Δ respectively. Of the 23 down‐regulated genes, 11 of 13 viable deletion mutants were identified to be tolerant to heat, suggesting that the down‐regulation of those genes might have contributed to the enhanced heat tolerance in <italic>dfg5</italic>Δ. Deletion of <italic>DFG</italic><italic>5</italic> caused slight activation of mitogen‐activated protein kinases Hog1 in the high‐osmolarity glycerol pathway and Slt2 in the cell wall integrity pathway. Therefore, a model is proposed on the signal transduction pathways associated with deletion of <italic>DFG</italic><italic>5</italic> upon heat stress.</p> </abstract>