Molecular cloning of a P-type ATPase gene from the cyanobacterium Synechocystis sp. PCC 6803. Homology to eukaryotic Ca(2+)-ATPases.
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.
Geisler
M
M
Institut für Biochemie der Pflanzen, Heinrich-Heine-Universität Düsseldorf, Germany.
Richter
J
J
Schumann
J
J
D000251:Adenosine Triphosphatases / Q000737:chemistry / Q000235:genetics*; D000595:Amino Acid Sequence; D000252:Calcium-Transporting ATPases / Q000737:chemistry; D003001:Cloning, Molecular; D000458:Cyanobacteria / Q000201:enzymology* / Q000235:genetics; D005796:Genes; D008969:Molecular Sequence Data; D010802:Phylogeny; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D012995:Solubility
D000251:Adenosine Triphosphatases; D000252:Calcium-Transporting ATPases