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A calmodulin‐stimulated Ca 2+ ‐ATPase from plant vacuolar membranes with a putative regulatory domain at its N‐terminus 1
Author(s) -
Malmström Susanna,
Askerlund Per,
Palmgren Michael G.
Publication year - 1997
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/s0014-5793(96)01448-2
Subject(s) - calmodulin , complementary dna , atpase , chloroplast , biochemistry , arabidopsis thaliana , biology , peptide sequence , microbiology and biotechnology , enzyme , gene , mutant
A cDNA, BCA1 , encoding a calmodulin‐stimulated Ca 2+ ‐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 Ca 2+ ‐ATPases and Arabidopsis thaliana ACA1 , that encodes a putative Ca 2+ pump in the chloroplast envelope. In contrast to the plasma membrane Ca 2+ ‐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.