Geisler M, Richter J, Schumann J
Institut für Biochemie der Pflanzen, Heinrich-Heine-Universität Düsseldorf, Germany.
J Mol Biol. 1993 Dec 20;234(4):1284-9. doi: 10.1006/jmbi.1993.1684.
With oligonucleotide primers derived from P-type ATPase genes of different sources, a part of Synechocystis sp. PCC 6803 genomic DNA was amplified and used as hybridization probe for the Synechocystis gene. A 4.7 kb HindIII fragment was cloned and sequenced; it contains the open reading frame of the E1E2-ATPase. The Synechocystis ATPase (named PMA1) consists of 915 amino acids with a M(r) of 98,902; it has ten putative transmembrane domains and contains the conserved regions a to j common to all P-type ATPases. Its amino acid sequence shows less than 20% identity to prokaryotic ATPases but about 30% identity to eukaryotic Ca(2+)-ATPases. An alignment to rat kidney and yeast Ca(2+)-ATPase protein sequences shows homology in stalk regions and transmembrane domains domains which are thought to be involved in calcium binding and transport; these three ATPases reveal very similar hydropathy plots and form a separate group in the phylogenetic tree of P-type ATPases. The results strongly support the assumption that PMA1 of Synechocystis is a calcium translocating ATPase, possibly involved in regulatory processes with calcium as second messenger.
利用来源于不同来源的P型ATP酶基因的寡核苷酸引物，对集胞藻PCC 6803基因组DNA的一部分进行了扩增，并将其用作集胞藻基因的杂交探针。克隆并测序了一个4.7 kb的HindIII片段；它包含E1E2 - ATP酶的开放阅读框。集胞藻ATP酶（命名为PMA1）由915个氨基酸组成，分子量为98,902；它有十个假定的跨膜结构域，并包含所有P型ATP酶共有的保守区域a到j。其氨基酸序列与原核ATP酶的同一性低于20%，但与真核Ca(2 +)-ATP酶的同一性约为30%。与大鼠肾脏和酵母Ca(2 +)-ATP酶蛋白质序列的比对显示，在被认为参与钙结合和运输的柄区和跨膜结构域中存在同源性；这三种ATP酶显示出非常相似的亲水性图谱，并在P型ATP酶的系统发育树中形成一个单独的组。结果有力地支持了这样一种假设，即集胞藻的PMA1是一种钙转运ATP酶，可能参与以钙作为第二信使的调节过程。
