Characterization of Neurospora crassa α-Actinin
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α-Actinin, an actin-binding protein of the spectrin superfamily, is present in most eukaryotes except plants. It is composed of three domains: N-terminal CH-domains, C-terminal calcium-binding domain (with EF-hand motifs), and a central rod domain. We have cloned and expressed Neurospora crassa α-actinin as GST and GFP fusion proteins for biochemical characterization and in vivo localization, respectively. The intracellular localization pattern of α-actinin suggests that this protein is intimately associated with actin filaments and plays an important role in the processes of germination, hyphal elongation, septum formation, and conidiation. These functions were confirmed by the experiments on the effect of α-actinin gene deletion in N. crassa.
We gratefully acknowledge financial support from the Academic Society of Geneva (F. B.). Thanks are due to R. Strasser for interest in the project and encouragement, M.-L. Chappuis for technical assistance and A. Fehr for secretarial assistance.
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