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Volume 271, Number 45, Issue of November 8, 1996 pp. 28366-28374
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Binding of Centrins and Yeast Calmodulin to Synthetic Peptides Corresponding to Binding Sites in the Spindle Pole Body Components Kar1p and Spc110p

(Received for publication, July 23, 1996, and in revised form, August 22, 1996)

From the Max-Planck-Institut für Biochemie, Genzentrum, Am Klopferspitz 18a, D-82152 Martinsried, Germany

Centrins contain four potential Ca²⁺ binding sites, known as EF-hands, and have essential functions in centrosome duplication and filament contraction. Here we report that centrins from yeast, green algae, and humans bound with high affinity to a peptide of the yeast centrosomal component Kar1p. Interestingly, centrin binding was regulated by physiological relevant changes in [Ca²⁺], and this Ca²⁺ dependence was influenced by acidic amino acids within the Kar1p peptide, which also prevented efficient binding of the related yeast calmodulin. However, a hybrid protein with the third and fourth EF-hands from the yeast centrin Cdc31p and the amino-terminal half from yeast calmodulin behaved more like Cdc31p, indicating that the carboxyl-terminal half of Cdc31p influences binding specificity. Besides Kar1p, centrins bound to a yeast calmodulin binding site, explaining the dosage-dependent suppression of a calmodulin mutant by CDC31. Consistent with an essential role of Ca²⁺ for centrin functions, mutations in the first or the fourth EF-hands of Cdc31p, impairing the Ca²⁺-induced conformational change of Cdc31p, resulted in nonfunctional proteins in vivo. Our results suggest that centrins are involved in Ca²⁺ signaling, likely by influencing the properties of target proteins in response to changes in [Ca²⁺].

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