Characterization of Avt1p as a vacuolar proton/amino acid antiporter in Saccharomyces cerevisiae
Characterization of Avt1p as a vacuolar proton/amino acid antiporter in Saccharomyces cerevisiae
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Avt1p 作为酿酒酵母液泡质子/氨基酸逆向转运蛋白的表征
DOI：
10.1080/09168451.2014.998621
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发表时间：
2015
影响因子：
1.6
通讯作者：
Yoshimi Kakinuma
中科院分区：
文献类型：
--
作者：
Junichi Tone;Ayumi Yoshimura;Kunio Manabe;Nami Murao;Takayuki Sekito;Miyuki Kawano-Kawada;Yoshimi Kakinuma
在酿酒酵母中已经报道了几个与氨基酸液泡转运有关的基因，但还没有得到很好的研究。我们鉴定了AVT 1，它是AVT空泡转运蛋白家族的一员，据报道与酵母的寿命有关。AVT输出突变体的空泡囊泡对异亮氨酸和组氨酸的ATP依赖性摄取因引入avt 1突变而丧失。V-ATP酶抑制剂：康卡霉素A和质子载体抑制摄取活性。各种中性氨基酸和组氨酸抑制异亮氨酸摄取，但γ-氨基丁酸、谷氨酸和天冬氨酸不抑制异亮氨酸摄取。V-ATP酶依赖的酸化的囊泡下降通过添加异亮氨酸或组氨酸，取决于Avt 1 p。结合细胞内液泡组分的氨基酸含量数据，表明Avt 1 p是一种质子/氨基酸逆向转运蛋白，对液泡内氨基酸的区室化具有重要作用。
Several genes for vacuolar amino acid transport were reported inSaccharomyces cerevisiae,but have not well been investigated. We characterizedAVT1, a member of the AVT vacuolar transporter family, which is reported to be involved in lifespan of yeast. ATP-dependent uptake of isoleucine and histidine by the vacuolar vesicles of an AVT exporter mutant was lost by introducingavt1∆ mutation. Uptake activity was inhibited by the V-ATPase inhibitor: concanamycin A and a protonophore. Isoleucine uptake was inhibited by various neutral amino acids and histidine, but not by γ-aminobutyric acid, glutamate, and aspartate. V-ATPase-dependent acidification of the vesicles was declined by the addition of isoleucine or histidine, depending upon Avt1p. Taken together with the data of the amino acid contents of vacuolar fractions in cells, the results suggested that Avt1p is a proton/amino acid antiporter important for vacuolar compartmentalization of various amino acids.