Mastoparan binding induces Ca(2+)-transfer between two globular domains of calmodulin: a 1H NMR study.

The interaction between calmodulin and mastoparan at various concentrations of calcium ions was studied by 1H NMR. It was found that at lower mastoparan concentrations 1 mol of mastoparan binds to both the C-terminal-half and N-terminal-half regions of calcium-saturated calmodulin. The mastoparan affinity is much greater for the C-terminal-half region than for the N-terminal-half region. At higher mastoparan concentrations, a further 1 mol of mastoparan binds to the N-terminal-region of calcium saturated calmodulin. The results can be interpreted in terms of the assumption that the N-terminal-half region of calmodulin with mastoparan has a higher calcium ion affinity than the C-terminal-half region without mastoparan. It is suggested that calcium ions transfer from the C-terminal-half region of calmodulin without mastoparan to the N-terminal-half region of calmodulin with mastoparan. This calcium ion transfer is discussed from the viewpoint of enzyme activation by calmodulin.