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Saccharomyces cerevisiae  calcineurin (CN) consists of a catalytic subunit CNA1 or CNA2 and a regulatory subunit CNB1. The kinetics of activation of yeast CN holoenzymes and their catalytic domains by Mn 2+  were investigated. We report that the  in vitro  phosphatase reaction activated by Mn 2+  typically has a pronounced initial lag phase caused by slow conformational rearrangement of the holoenzyme-Mn 2+ . A similar lag phase was detected using just the catalytic domain of yeast CN, indicating that the slowness of Mn 2+ -induced conformational change of CN results from a rearrangement within the catalytic domain. The Mn 2+ -activation of CN was reversible. The dissociation constant of the CN heterodimer containing the CNA2 subunit in the presence of Mn 2+  was 3-fold higher than that of CN containing the CNA1 subunit and that of the catalytic domains of CNA1 and CNA2, pointing to differences between the residues surrounding the Mn 2+ -binding sites of CNA1 and CNA2.

Mechanism of activation of Saccharomyces cerevisiae calcineurin by Mn 2+