Characterisation of Schizosaccharomyces pombe α-actinin

PeerJ

Barbara Addario¹  Karina Persson²  Lars Backman²  Linda Sandblad³ 

[1] Cell Biology Laboratory, School of Biochemistry and Cell Biology, BioScience Institute, University College Cork, Cork, Ireland;Department of Chemistry, Biological Chemistry, Umeå, Sweden;Department of Molecular Biology, UmeåUniversity, Umeå, Sweden;

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

DOI  :  10.7717/peerj.1858

来源: DOAJ

【 摘 要 】

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.

【 授权许可】

Unknown