Characterisation of Schizosaccharomyces pombe α-actinin
No Thumbnail Available
The actin cytoskeleton plays a fundamental role in eukaryotic cells. Its reorganization is regulated by a plethora of actin-modulating proteins, such as a-actinin. In higher organisms, α-actinin is characterized by the presence of three distinct structural domains: an N-terminal actin-binding domain and a C-terminal region with EF-hand motif separated by a central rod domain with four spectrin repeats. Sequence analysis has revealed that the central rod domain of α-actinin from the fission yeast Schizosaccharomyces pombe consists of only two spectrin repeats. To obtain a firmer understanding of the structure and function of this unconventional α-actinin, we have cloned and characterized each structural domain. Our results show that this a-actinin isoform is capable of forming dimers and that the rod domain is required for this. However, its actin-binding and cross-linking activity appears less efficient compared to conventional α-actinins. The solved crystal structure of the actin-binding domain indicates that the closed state is stabilised by hydrogen bonds and a salt bridge not present in other α-actinins, which may reduce the affinity for actin.
Spectrin repeat , Actin-binding protein , α-actinin , Schizosaccharomyces pombe
Addario, B., Sandblad, L., Persson, K. and Backman, L. (2016) 'Characterisation of Schizosaccharomyces pombe α-actinin', PeerJ, 4, pp. e1858. doi:10.7717/peerj.1858
© 2016 Addario et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, reproduction and adaptation in any medium and for any purpose provided that it is properly attributed. For attribution, the original authors, title, publication source (PeerJ) and either DOI or URL of the article must be cited.