The C-terminal domain of TPX2 is made of alpha-helical tandem repeats

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• dc.contributor.author Sanchez-Pulido, Luisca
• dc.contributor.author Perez, Laurentca
• dc.contributor.author Kuhn, Steffenca
• dc.contributor.author Vernos, Isabelle, 1959-ca
• dc.contributor.author Andrade-Navarro, Miguel A.ca
• dc.date.accessioned 2017-01-13T08:22:59Z
• dc.date.available 2017-01-13T08:22:59Z
• dc.date.issued 2016ca
• dc.description.abstract Background: TPX2 (Targeting Protein for Xklp2) is essential for spindle assembly, activation of the mitotic kinase Aurora A and for triggering microtubule nucleation. Homologs of TPX2 in Chordata and plants were previously identified. Currently, proteins of the TPX2 family have little structural information and only small parts are covered by defined protein domains. Methods: We have used computational sequence analyses and structural predictions of proteins of the TPX2 family, supported with Circular Dichroism (CD) measurements. Results: Here, we report our finding that the C-terminal domain of TPX2, which is responsible of its microtubule nucleation capacity and is conserved in all members of the family, is actually formed by tandem repeats, covering well above 2/3 of the protein. We propose that this region forms a flexible solenoid involved in protein-protein interactions. Structural prediction and molecular modeling, combined with Circular Dichroism (CD) measurements reveal a predominant alpha-helical content. Furthermore, we identify full length homologs in fungi and shorter homologs with a different domain organization in diptera (including a paralogous expansion in Drosophila). Conclusions: Our results, represent the first computational and biophysical analysis of the TPX2 proteins family and help understand the structure and evolution of this conserved protein family to direct future structural studies.
• dc.format.mimetype application/pdfca
• dc.identifier.citation Sanchez-Pulido L, Perez L, Kuhn S, Vernos I, Andrade-Navarro MA. The C-terminal domain of TPX2 is made of alpha-helical tandem repeats. BMC Structural Biology. 2016; 16(1): 17. DOI: 10.1186/s12900-016-0070-8ca
• dc.identifier.doi http://dx.doi.org/10.1186/s12900-016-0070-8
• dc.identifier.issn 1472-6807ca
• dc.identifier.uri http://hdl.handle.net/10230/27882
• dc.language.iso engca
• dc.publisher BioMed Centralca
• dc.relation.ispartof BMC Structural Biology. 2016; 16(1): 17
• dc.rights © The Author(s). 2016. Open Access. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.ca
• dc.rights.accessRights info:eu-repo/semantics/openAccessca
• dc.rights.uri http://creativecommons.org/licenses/by/4.0/
• dc.subject.keyword TPX2
• dc.subject.keyword Protein sequence tandem repeats
• dc.subject.keyword Protein sequence analysis
• dc.subject.keyword Protein structure prediction
• dc.subject.keyword Alpha-solenoid
• dc.subject.keyword Circular Dichroism
• dc.title The C-terminal domain of TPX2 is made of alpha-helical tandem repeatsca
• dc.type info:eu-repo/semantics/articleca
• dc.type.version info:eu-repo/semantics/publishedVersionca