Open AccessComparison of the influence of small GTP ases A rl1 and Y pt6 on yeast cells’ tolerance to various stress factors
Author(s) -
Marešová Lydie,
Vydarený Tomáš,
Sychrová Hana
Publication year - 2012
Publication title -
fems yeast research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.991
H-Index - 92
eISSN - 1567-1364
pISSN - 1567-1356
DOI - 10.1111/j.1567-1364.2011.00780.x
Subject(s) - gtpase , saccharomyces cerevisiae , hygromycin b , biology , mutant , antiporter , golgi apparatus , phenotype , small gtpase , intracellular , biochemistry , yeast , microbiology and biotechnology , gene , membrane , cell , signal transduction
The GTP ases A rl1 and Y pt6 are involved in the intracellular transport of vesicles and their fusion with the trans‐ G olgi network. This work is focused on comparing the roles of these GTP ases in the tolerance of S accharomyces cerevisiae cells to an increased concentration of alkali metal cations and other stress factors. We studied the phenotypes of arl1 or ypt6 deletions in combination with the deletions of genes encoding alkali‐metal‐cation transporters ( ena1‐4 , nha1 , nhx1 , and kha1 ). Salt sensitivity of the arl1 and ypt6 mutants was shown to be independent of the tested cation transporters and electrochemical membrane potential. Phenotype manifestations of ypt6 deletion were usually more prominent than those of arl1 (cells were more sensitive to KCl , NaCl , LiCl , hygromycin B , increased temperature, and increased p H ). At suboptimal temperature, the growth inhibition of arl1 and ypt6 mutants was approximately the same, and low p H was the only condition where arl1 mutants grew even worse than ypt6 mutants. Overexpression of the ARL1 gene suppressed the phenotypes of ypt6 deletion; however, this did not work vice versa (additional copies of YPT6 could not replace ARL1 ). Our results suggest partially overlapping functions of the GTP ases in resistance to various stress factors, with Y pt6 being more efficient under physiological conditions and A rl1 more versatile when overexpressed.