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Amplification of the phosphorylation site ‐ ATP‐binding site cDNA fragment of the Na + ,K + ‐ATPase and the Ca 2+ ‐ATPase of Drosophila melanogaster by polymerase chain reaction
Author(s) -
Váradi András,
Gilmore-Heber Maureen,
Benz Edward J.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81653-9
Subject(s) - microbiology and biotechnology , atpase , complementary dna , biology , endoplasmic reticulum , p type atpase , dna , gene , oligonucleotide , calcium atpase , drosophila melanogaster , biochemistry , enzyme
In vitro DNA‐amplification technique has been utilized to generate a 430 bp fragment of the Na + ,K + ‐ATPase, and a 550 bp fragment of a Ca 2+ ‐ATPase (the sarcoplasmic reticulum‐type) of Drosophila melanogaster . The oligonucleotide primers for the DNA‐amplification (Polymerase Chain Reaction) had been designed on the basis of amino acid sequence motifs ‐ the phosphorylation site and the ATP‐binding site ‐ conserved among members of the ATPase protein family. Using the amplified cDNA‐segments as probes, we demonstrated that there is one Na + ,K + ‐ATPase and one Ca 2+ ‐ATPase (sarcoplasnaic reticulum‐type) gene in the Drosophila genome. Three different mRNA species are processed from the Na + ,K + ‐ATPase gene and one from the Ca 2+ ‐ATPase gene. Developmental control in expression of the Ca 2+ ‐ATPase gene was observed.