A calmodulin-stimulated Ca-ATPase from plant vacuolar membranes with a putative regulatory domain at its N-terminus |
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| Authors: | Susanna Malmström Per Askerlund Michael G Palmgren |
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| Institution: | aMolecular Biology Institute, Copenhagen University, Øster Farimagsgade 2A, DK-1353 Copenhagen K, Denmark;bDepartment of Plant Biology, The Royal Veterinary and Agricultural University, Thorvaldsensvej 40, DK-1871 Frederiksberg C, Denmark;cDepartment of Plant Biochemistry, Lund University, P.O. Box 117, S-221 00 Lund, Sweden |
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| Abstract: | 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. |
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| Keywords: | Signal transduction Calcium Pump Vacuole |
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