Rudolph H K, Antebi A, Fink G R, Buckley C M, Dorman T E, LeVitre J, Davidow L S, Mao J I, Moir D T
Whitehead Institute for Biomedical Research Cambridge, Massachusetts 02142.
Cell. 1989 Jul 14;58(1):133-45. doi: 10.1016/0092-8674(89)90410-8.
The genes for two new P-type ATPases, PMR1 and PMR2, have been identified in yeast. A comparison of the deduced sequences of the PMR proteins with other known ion pumps showed that both proteins are very similar to Ca2+ ATPases. PMR1 is identical to SSC1, a gene previously identified by its effect on secretion of some foreign proteins from yeast. Proteins secreted from pmr1 mutants lack the outer chain glycosylation that normally results from passage through the Golgi. Loss of PMR1 function suppresses the lethality of ypt1-1, a mutation that blocks the secretion pathway. These data suggest that PMR1 functions as a Ca2+ pump affecting transit through the secretory pathway.
在酵母中已鉴定出两种新的P型ATP酶基因PMR1和PMR2。将PMR蛋白的推导序列与其他已知离子泵进行比较，结果表明这两种蛋白与Ca2+ ATP酶非常相似。PMR1与SSC1相同，SSC1是先前因其对酵母中某些外源蛋白分泌的影响而鉴定出的一个基因。从pmr1突变体分泌的蛋白缺乏正常情况下通过高尔基体所产生的外链糖基化。PMR1功能的丧失抑制了ypt1-1的致死性，ypt1-1是一种阻断分泌途径的突变。这些数据表明PMR1作为一种Ca2+泵发挥作用，影响分泌途径中的转运。
