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Volume 271, Number 37, Issue of September 13, 1996 pp. 22453-22461
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Characterization of Green Alga, Yeast, and Human Centrins
SPECIFIC SUBDOMAIN FEATURES DETERMINE FUNCTIONAL DIVERSITY

(Received for publication, April 16, 1996, and in revised form, June 29, 1996)

Hans Wiech , Birgitta M. Geier , Thilo Paschke , Anne Spang , Katrin Grein , Jutta Steinkötter ^¶ , Michael Melkonian ^¶ and Elmar Schiebel

From the  Max-Planck-Institut für Biochemie, Genzentrum, Am Klopferspitz 18a, 82152 Martinsried and the ^¶ Universität zu Köln, Botanisches Institut, Gyrhofstrasse 15, 50931 Köln, Federal Republic of Germany

Centrins are a subfamily within the superfamily of Ca²⁺-modulated proteins that play a fundamental role in centrosome duplication and contraction of centrin-based fiber systems. We examined the individual molecular properties of yeast, green alga, and human centrins. Circular dichroism spectroscopy revealed a divergent influence of Ca²⁺ binding on the -helical content of these proteins. Ca²⁺-free centrins were elongated in shape as determined by size exclusion chromatography. The presence of Ca²⁺ and binding peptide resulted in more spherical shaped centrins. In contrast to yeast calmodulin, centrins formed multimers in the Ca²⁺-bound state. This oligomerization was significantly reduced in the absence of Ca²⁺ and in the presence of binding peptide. The Ca²⁺-dependent polymerization of the green alga Scherffelia dubia centrin (SdCen) resulted in a filamentous network. This molecular property was mainly dependent on the amino-terminal subdomain and the peptide-binding site of SdCen. Finally, we analyzed whether SdCen and Cdc31p-SdCen hybrid proteins functionally substitute for the Saccharomyces cerevisiae centrin Cdc31p. Only hybrid proteins containing the amino-terminal subdomain or the third EF-hand of SdCen and the other subdomains from Cdc31p were functional in vivo.

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