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Cloning and Molecular Analysis of the Plasma Membrane Ca 2+ ‐ATPase Gene in Paramecium tetraurelia
Author(s) -
ELWESS NANCY L.,
VAN HOUTEN JUDITH L.
Publication year - 1997
Publication title -
journal of eukaryotic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 1066-5234
DOI - 10.1111/j.1550-7408.1997.tb05708.x
Subject(s) - paramecium , biology , calmodulin , atpase , plasma membrane ca2+ atpase , gene , homology (biology) , p type atpase , molecular cloning , biochemistry , peptide sequence , membrane , microbiology and biotechnology , enzyme
. We have determined the DNA sequence of the gene encoding the protein of the plasma membrane Ca 2+ ‐ATPase in Paramecium tetraurelia . The predicted amino acid sequence of the plasma membrane Ca 2+ ‐ATPase shows homology to conserved regions of known plasma membrane Ca 2+ ‐ATPases and contains the known binding sites for ATP (FITC), acylphosphate formation, and calmodulin, as well as the “hinge” region: all characteristics common to plasma membrane Ca 2+ ‐ATPases. The deduced molecular weight for this sequence is 131 kDa. The elucidation of this gene will assist in the studies of the mechanisms by which this excitable cell removes calcium entering through voltage gated calcium channels and the pump functions in chemosensory signal transduction.