| Literature DB >> 26325352 |
Miyuki Kawano-Kawada1,2, Pongsanat Pongcharoen1, Rieko Kawahara1, Mayu Yasuda1, Takashi Yamasaki1, Koichi Akiyama1,2, Takayuki Sekito1, Yoshimi Kakinuma1.
Abstract
In the vacuolar basic amino acid (VBA) transporter family of Saccharomyces cerevisiae, VBA4 encodes a vacuolar membrane protein with 14 putative transmembrane helices. Transport experiments with isolated vacuolar membrane vesicles and estimation of the amino acid contents in vacuoles showed that Vba4p is not likely involved in the transport of amino acids. We found that the vba4Δ cells, as well as vba1Δ and vba2Δ cells, showed increased susceptibility to several drugs, particularly to azoles. Although disruption of the VBA4 gene did not affect the salt tolerance of the cells, vacuolar fragmentation observed under high salt conditions was less prominent in vba4Δ cells than in wild type, vba1Δ, and vba2Δ cells. Vba4p differs from Vba1p and Vba2p as a vacuolar transporter but is important for the drug resistance and vacuolar morphology of S. cerevisiae.Entities:
Keywords: azole; multidrug resistance; vacuolar transporter
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Year: 2015 PMID: 26325352 DOI: 10.1080/09168451.2015.1083401
Source DB: PubMed Journal: Biosci Biotechnol Biochem ISSN: 0916-8451 Impact factor: 2.043