Amplification of the phosphorylation site - ATP-binding site cDNA fragment of the Na+,K+-ATPase and the Ca2+-ATPase of Drosophila melanogaster by polymerase chain reaction

A. Váradi, Maureen Gilmore-Heber, Edward J. Benz

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

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 Ca2+-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 Ca2+-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 Ca2+-ATPase gene. Developmental control in expression of the Ca2+-ATPase gene was observed.

Original languageEnglish
Pages (from-to)203-207
Number of pages5
JournalFEBS Letters
Volume258
Issue number2
DOIs
Publication statusPublished - Dec 4 1989

Fingerprint

Phosphorylation
Calcium-Transporting ATPases
Polymerase chain reaction
Drosophila melanogaster
Amplification
Complementary DNA
Genes
Adenosine Triphosphate
Binding Sites
Adenosine Triphosphatases
Polymerase Chain Reaction
Nucleic Acid Amplification Techniques
Reticulum
Amino Acid Motifs
DNA Primers
Sarcoplasmic Reticulum
DNA-Directed DNA Polymerase
Drosophila
Amino Acid Sequence
Genome

Keywords

  • (Drosophila melanogaster)
  • ATPase
  • Developmental control of gene expression
  • Homology primer
  • Polymerase chain reaction

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Amplification of the phosphorylation site - ATP-binding site cDNA fragment of the Na+,K+-ATPase and the Ca2+-ATPase of Drosophila melanogaster by polymerase chain reaction. / Váradi, A.; Gilmore-Heber, Maureen; Benz, Edward J.

In: FEBS Letters, Vol. 258, No. 2, 04.12.1989, p. 203-207.

Research output: Contribution to journalArticle

@article{386eb8711f4a4469b086665b6bbe515e,
title = "Amplification of the phosphorylation site - ATP-binding site cDNA fragment of the Na+,K+-ATPase and the Ca2+-ATPase of Drosophila melanogaster by polymerase chain reaction",
abstract = "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 Ca2+-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 Ca2+-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 Ca2+-ATPase gene. Developmental control in expression of the Ca2+-ATPase gene was observed.",
keywords = "(Drosophila melanogaster), ATPase, Developmental control of gene expression, Homology primer, Polymerase chain reaction",
author = "A. V{\'a}radi and Maureen Gilmore-Heber and Benz, {Edward J.}",
year = "1989",
month = "12",
day = "4",
doi = "10.1016/0014-5793(89)81653-9",
language = "English",
volume = "258",
pages = "203--207",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "2",

}

TY - JOUR

T1 - Amplification of the phosphorylation site - ATP-binding site cDNA fragment of the Na+,K+-ATPase and the Ca2+-ATPase of Drosophila melanogaster by polymerase chain reaction

AU - Váradi, A.

AU - Gilmore-Heber, Maureen

AU - Benz, Edward J.

PY - 1989/12/4

Y1 - 1989/12/4

N2 - 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 Ca2+-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 Ca2+-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 Ca2+-ATPase gene. Developmental control in expression of the Ca2+-ATPase gene was observed.

AB - 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 Ca2+-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 Ca2+-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 Ca2+-ATPase gene. Developmental control in expression of the Ca2+-ATPase gene was observed.

KW - (Drosophila melanogaster)

KW - ATPase

KW - Developmental control of gene expression

KW - Homology primer

KW - Polymerase chain reaction

UR - http://www.scopus.com/inward/record.url?scp=0024326442&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0024326442&partnerID=8YFLogxK

U2 - 10.1016/0014-5793(89)81653-9

DO - 10.1016/0014-5793(89)81653-9

M3 - Article

VL - 258

SP - 203

EP - 207

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 2

ER -