Abstract
In order to elucidate a role of a putative EF-hand motif (144-172) in phospholipase C-δ1 (PLC-δ1), deletion and point mutation of the enzyme were performed and the mutated cDNAs were expressed in CHO cells and E. coli AD202 strain. Deletion of amino acid residues of 141-236 or 173-236 resulted in abolition of PLC activity. However, the decreased PLC activity to 15-20% by deletion of the EF-hand motif (144-172) was still Ca 2+-dependent. Furthermore, mutants, in which conserved Asp 153, Asp 157, Glu 164 or all these acidic amino acids in the EF-hand motif were replaced with alanine residues, showed nearly the same PLC activity and Ca 2+-dependency as those of wild-type. These results suggest that the region containing the EF-hand motif may not play a role in regulation of Ca 2+-sensitivity of PLC-δ1, but is important for its activity.
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