Calcium-Binding Proteins in Fungi and Higher Plants

Abstract

Calcium has long been known to be required for many vital processes in fungi and plants. High levels of calcium are found in cell walls, vacuoles, and most organelles. In contrast, very low levels of calcium are present in the cytosol of fungal and plant cells. The most recent evidence indicates that calcium is a true second messenger in fungi and plants. Because cyclic AMP does not appear to be a second messenger in plants, calcium is the only known second messenger. Calcium-binding proteins are involved in the events that accompany the action of calcium as a second messenger; three types have been identified in fungi and plants. The first group includes several proteins that bind 45 Ca2+ and are not known to have any enzymatic activity. A second type includes the many enzymes from fungi and plants stimulated by millimolar levels of calcium. The third type of calcium-binding protein, calmodulin, responds to micromolar levels of Ca2+ by binding to certain enzymes and stimulating them. Calmodulin has been detected in every eukaryote thus far examined. The amino acid composition of several fungal and plant calmodulins have been elucidated and found to be very similar to calmodulin from animals. Eight enzymes from fungi and plants have been reported to be regulated either directly or indirectly by calmodulin. Calmodulin antagonists have been used to study the possible involvement of calmodulin in many cellular processes in fungi and plants. Recently, several endogenous calmodulin antagonists have been identified in fungi and plants. The physiological significance of these compounds is currently being evaluated.