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A calmodulin-stimulated Ca2+-ATPase from plant vacuolar membranes with a putative regulatory domain at its N-terminus
Molecular Biology Institute, Copenhagen University, Copenhagen, Denmark.
Jönköping University, School of Education and Communication, HLK, Disciplinary Research. Department of Plant Biochemistry, Lund University, Lund, Sweden.ORCID iD: 0000-0003-0117-2974
Molecular Biology Institute, Copenhagen University, Copenhagen, Denmark.
1997 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 400, no 3, p. 324-328Article in journal (Refereed) Published
Abstract [en]

A cDNA, BCA1, encoding a calmodulin-stimulated Ca2+-ATPase in the vacuolar membrane of cauliflower (Brassica oleracea) was isolated based on the sequence of tryptic peptides derived from the purified protein. The BCA1 cDNA shares sequence identity with animal plasma membrane Ca2+-ATPases and Arabidopsis thaliana ACA1, that encodes a putative Ca2+ pump in the chloroplast envelope. In contrast to the plasma membrane Ca2+-ATPases of animal cells, which have a calmodulin-binding domain situated in the carboxy-terminal end of the molecule, the calmodulin-binding domain of BCA1 is situated at the amino terminus of the enzyme.

Place, publisher, year, edition, pages
1997. Vol. 400, no 3, p. 324-328
Keywords [en]
Amino Acid Sequence, Animals, Arabidopsis/enzymology/genetics, Brassica/*enzymology/genetics, Calcium-Transporting ATPases/*chemistry/*genetics/metabolism, Calmodulin/*metabolism, DNA; Complementary/genetics, Genes; Plant, Intracellular Membranes/enzymology, Molecular Sequence Data, Molecular Weight, Polymerase Chain Reaction, Protein Structure; Secondary, Sequence Homology; Amino Acid, Vacuoles/*enzymology
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:hj:diva-2174DOI: 10.1016/S0014-5793(96)01448-2PubMedID: 9009223OAI: oai:DiVA.org:hj-2174DiVA, id: diva2:32994
Available from: 2007-10-17 Created: 2007-10-17 Last updated: 2017-12-12Bibliographically approved

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