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Addario B, Sandblad L, Persson K, et al. Characterisation of Schizosaccharomyces pombe α-actinin. PeerJ. 2016;4:e1858doi: 10.7717/peerj.1858.
Addario, B., Sandblad, L., Persson, K., & Backman, L. (2016). Characterisation of Schizosaccharomyces pombe α-actinin. PeerJ, 4e1858. https://doi.org/10.7717/peerj.1858
Addario, Barbara, et al. "Characterisation of Schizosaccharomyces pombe α-actinin." PeerJ vol. 4 (2016): e1858. doi: https://doi.org/10.7717/peerj.1858
Addario B, Sandblad L, Persson K, Backman L. Characterisation of Schizosaccharomyces pombe α-actinin. PeerJ. 2016 Mar 28;4:e1858. doi: 10.7717/peerj.1858. eCollection 2016. PMID: 27069798; PMCID: PMC4824898.
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PeerJ. 2016 Mar 28;4:e1858. doi: 10.7717/peerj.1858. eCollection 2016.

Characterisation of Schizosaccharomyces pombe α-actinin.

PeerJ

Barbara Addario, Linda Sandblad, Karina Persson, Lars Backman

Affiliations

  1. Cell Biology Laboratory, School of Biochemistry and Cell Biology, BioScience Institute, University College Cork , Cork , Ireland.
  2. Department of Molecular Biology, UmeåUniversity , Umeå , Sweden.
  3. Department of Chemistry, Biological Chemistry , Umeå , Sweden.

PMID: 27069798 PMCID: PMC4824898 DOI: 10.7717/peerj.1858

Abstract

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.

Keywords: Actin-binding protein; Schizosaccharomyces pombe; Spectrin repeat; α-actinin

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