Characterisation of Schizosaccharomyces pombe α-actinin

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dc.contributor.author Addario, Barbara
dc.contributor.author Sandblad, Linda
dc.contributor.author Persson, Karina
dc.contributor.author Backman, Lars
dc.date.accessioned 2017-02-24T12:18:19Z
dc.date.available 2017-02-24T12:18:19Z
dc.date.issued 2016-03-28
dc.identifier.citation 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 en
dc.identifier.volume 4 en
dc.identifier.startpage e1858-1 en
dc.identifier.endpage e1858-22 en
dc.identifier.issn 2167-8359
dc.identifier.uri http://hdl.handle.net/10468/3689
dc.identifier.doi 10.7717/peerj.1858
dc.description.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. en
dc.format.mimetype application/pdf en
dc.language.iso en en
dc.publisher PeerJ en
dc.rights © 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. en
dc.rights.uri https://creativecommons.org/licenses/by/4.0/ en
dc.subject Spectrin repeat en
dc.subject Actin-binding protein en
dc.subject α-actinin en
dc.subject Schizosaccharomyces pombe en
dc.title Characterisation of Schizosaccharomyces pombe α-actinin en
dc.type Article (peer-reviewed) en
dc.internal.authorcontactother Barbara Addario, Cell Biology Laboratory, School of Biochemistry and Cell Biology, Biosciences Institute, University College Cork, T: +353 21 490 3000; E: baddario@ucc.ie en
dc.internal.availability Full text available en
dc.description.version Published Version en
dc.contributor.funder Carl Tryggers Stiftelse för Vetenskaplig Forskning en
dc.description.status Peer reviewed en
dc.identifier.journaltitle PeerJ en
dc.internal.IRISemailaddress baddario@ucc.ie en


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© 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. Except where otherwise noted, this item's license is described as © 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.
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