Polyamine Uptake by DUR3 and SAM3 in Saccharomyces cerevisiae*
Polyamine Uptake by DUR3 and SAM3 in Saccharomyces cerevisiae*
复制标题
DOI：
10.1074/jbc.m611105200
复制
发表时间：
2007-03
影响因子：
4.8
通讯作者：
T. Uemura;K. Kashiwagi;K. Igarashi
中科院分区：
文献类型：
--
作者：
T. Uemura;K. Kashiwagi;K. Igarashi
据报道，GAP1和AGP2在酿酒酵母中催化多胺和氨基酸的摄取。我们在酿酒酵母中寻找多胺优先摄取蛋白。DUR3与尿素一起催化多胺的摄取，SAM3与s -腺苷蛋氨酸、谷氨酸和赖氨酸一起催化多胺的摄取。在DUR3-和sam3缺陷细胞中，多胺摄取都大大减少。DUR3的腐胺和亚精胺Km分别为479和21.2 μm， SAM3的腐胺和亚精胺Km分别为433和20.7 μm。多胺对缺乏鸟氨酸脱羧酶的多胺需要突变体细胞生长的刺激不受GAP1和AGP2破坏的影响，但被DUR3和SAM3破坏而减弱。此外，多胺对需要多胺的突变体细胞生长的刺激被DUR3和SAM3的破坏完全抑制。结果表明，DUR3和SAM3是酵母主要的多胺摄取蛋白。我们以前报道过多胺转运蛋白激酶2调节多胺转运。发现DUR3（而不是SAM3）被多胺转运蛋白激酶2磷酸化Thr250， Ser251和Thr684激活。
It has been reported that GAP1 and AGP2 catalyze the uptake of polyamines together with amino acids in Saccharomyces cerevisiae. We have looked for polyamine-preferential uptake proteins in S. cerevisiae. DUR3 catalyzed the uptake of polyamines together with urea, and SAM3 was found to catalyze the uptake of polyamines together with S-adenosylmethionine, glutamic acid, and lysine. Polyamine uptake was greatly decreased in both DUR3- and SAM3-deficient cells. The Km values for putrescine and spermidine of DUR3 were 479 and 21.2 μm, respectively, and those of SAM3 were 433 and 20.7 μm, respectively. Polyamine stimulation of cell growth of a polyamine requiring mutant, which is deficient in ornithine decarboxylase, was not influenced by the disruption of GAP1 and AGP2, but it was diminished by the disruption of DUR3 and SAM3. Furthermore, the polyamine stimulation of cell growth of a polyamine-requiring mutant was completely inhibited by the disruption of both DUR3 and SAM3. The results indicate that DUR3 and SAM3 are major polyamine uptake proteins in yeast. We previously reported that polyamine transport protein kinase 2 regulates polyamine transport. It was found that DUR3 (but not SAM3) was activated by phosphorylation of Thr250, Ser251, and Thr684 by polyamine transport protein kinase 2.