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Characterization of Neurospora crassa α-Actinin

Published inCurrent Microbiology, vol. 63, no. 1, p. 100-105
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  • Open Access - Licence nationale Springer 
Publication date2011
Abstract

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.

Citation (ISO format)
COTADO SAMPAYO, Marta et al. Characterization of Neurospora crassa α-Actinin. In: Current Microbiology, 2011, vol. 63, n° 1, p. 100–105. doi: 10.1007/s00284-011-9954-9
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