Molecular Cloning of a P-type ATPase Gene from the Cyanobacterium Synechocystis sp. PCC 6803: Homology to Eukaryotic Ca2+-ATPases

摘要: Abstract With oligonucleotide primers derived from P-type ATPase genes of different sources, a part Synechocystis sp. PCC 6803 genomic DNA was amplified and used as hybridization probe for the gone. A 4·7 kb Hin dIII fragment cloned sequenced; it contains open reading frame E 1 2 -ATPase. The (named PM A1 ) consists 915 amino acids with M r 98,902; has ten putative transmembrane domains conserved regions to j common all ATPases. Its acid sequence shows less than 20% identity prokaryotic ATPases but about 30% eukaryotic Ca 2+ -ATPases. An alignment rat kidney yeast -ATPase protein sequences homology in stalk which are thought be involved calcium binding transport; these three reveal very similar hydropathy plots form separate group phylogenetic tree results strongly support assumption that is translocating ATPase, possibly regulatory processes second messenger.