Cavero Santiago, Traba Javier, Del Arco Araceli, Satrústegui Jorgina
Departamento de Biología Molecular, Centro de Biología Molecular Severo Ochoa UAM-CSIC, Facultad de Ciencias, Universidad Autónoma, 28049 Madrid, Spain.
Biochem J. 2005 Dec 15;392(Pt 3):537-44. doi: 10.1042/BJ20050806.
Sal1p is a mitochondrial protein that belongs to the SCaMC (short calcium-binding mitochondrial carrier) subfamily of mitochondrial carriers. The presence of calcium-binding motifs facing the extramitochondrial space allows the regulation of the transport activity of these carriers by cytosolic calcium and provides a new mechanism to transduce calcium signals in mitochondria without the requirement of calcium entry in the organelle. We have studied its transport activity, finding that it is a carboxyatractyloside-resistant ATP-Mg carrier. Mitochondria from a disruption mutant of SAL1 have a 50% reduction in the uptake of ATP. We have also found a clear stimulation of ATP-transport activity by calcium, with an S(0.5) of approx. 30 microM. Our results also suggest that Sal1p is a target of the glucose-induced calcium signal which is non-essential in wild-type cells, but becomes essential for transport of ATP into mitochondria in yeast lacking ADP/ATP translocases.
Sal1p是一种线粒体蛋白,属于线粒体载体的SCaMC(短钙结合线粒体载体)亚家族。面向线粒体外空间的钙结合基序的存在使得这些载体的转运活性能够受到胞质钙的调节,并提供了一种在线粒体中传导钙信号的新机制,而无需钙进入细胞器。我们研究了它的转运活性,发现它是一种对羧基苍术苷抗性的ATP-Mg载体。来自SAL1缺失突变体的线粒体对ATP的摄取减少了50%。我们还发现钙能明显刺激ATP转运活性,其半最大效应浓度(S(0.5))约为30微摩尔。我们的结果还表明,Sal1p是葡萄糖诱导的钙信号的靶点,这在野生型细胞中并非必需,但在缺乏ADP/ATP转位酶的酵母中,对于ATP转运到线粒体中变得至关重要。