A tandem pair of Leishmania donovani cation transporting ATPase genes encode isoforms that are differentially expressed

IDENTIFICATION AND DNA SEQUENCE OF A NEW H+‐ATPase IN THE UNICELLULAR GREEN ALGA CHLAMYDOMONAS REINHARDTII (CHLOROPHYCEAE)

“…This partial cDNA was sequenced to completion and was found to consist of 1.2 kb of coding sequence and 1 kb of 3′ untranslated region. The predicted 400 amino acids encoded by the partial cDNA displayed 38% identity and 53% similarity to the carboxyl terminus of the proton transporting ATPase LDH1A from Leishmania donovani (Meade et al 1987, 1989). This relatively high similarity at the carboxyl terminus was surprising because this region generally shows the greatest amount of divergence within the family of H + ‐ATPases (e.g.…”

Membrane Proteins and Enzymes of Leishmania

“…Finally, the membrane location of a protein can, with some degree of success, be deduced from the primary structure of the protein predicted from the gene sequence. The predicted amino acid sequence may indicate a hydrophobic polypeptide domain, multiple membrane spanning domains, or a signal for glycosyl-phosphatidylinositol addition at the COOH-terminus, or other similarities to membrane proteins characterized from other organisms (Bard, 1989;Cairns et al, 1989;Murray et al, 1989a;Meade et al, 1987Meade et al, , 1989Ouellette et al, 1990;Stein et al, 1990). …”

“…These genes, which were detected in four Leishmania species, are disposed head-to-tail on a small 750-kb chromosome. The genes were cloned, sequenced, and the deduced amino acid sequences were shown to be similar to both yeast and mammalian ATPases, with ten predicted transmembrane segments (Meade et al, 1987(Meade et al, , 1989(Meade et al, , 1991. The two Leishmania gene products differ in 20 amino acids out of 974, with 15 changes occurring near the carboxyl terminus, adding three positive charges and a second potential glycosylation site in ATPase lb.…”

Molecular Biology of the Plasma Membrane of Higher Plants

“…zyme and amino acid sequence data all indicate that the plant plasma membrane proton pump belongs to the Ptype class of proton pumps (Schaller and Sussman, 1988b). Other well-characterized members of this group whose genes have been cloned and sequenced include (1) the fungal plasma membrane proton pump (H+-ATPase) (Hager et al, 1986;Serrano, Kielland-Brandt, and Fink, 1986) as well as a putative proton pump in the plasma membrane of the protozoan, Leishmania donovani (Meade et al, 1989); (2) the Na+,K+-ATPase in mammalian plasma membrane (Shull, Schwartz, and Lingrell, 1985;Shull and Lingrel, 1987); (3) the K+-ATPase of bacterial plasma mem? branes (Walderhaug, Litwack, and Epstein, 1989); (4) an FT.rC-ATPase in mammalian stomach (Shull and Lingrel, 1986;Maeda, Ishizaki, and Futai, 1988); (5) the Ca2+-ATPase of mammalian plasma membrane (Shull and Greeb, 1988;Verma et al, 1988); and (6) the Ca2+-ATPase of mammalian sarcoplasmic and endoplasmic reticulum (MacLennan et al, 1985;Brandl et al, 1986;Lytton and MacLennan, 1988;Lytton et al, 1989).…”