University of Oulu

Ábris Ádám Bendes, Moon Chatterjee, Benjamin Götte, Petri Kursula, Inari Kursula, Functional homo- and heterodimeric actin capping proteins from the malaria parasite, Biochemical and Biophysical Research Communications, Volume 525, Issue 3, 2020, Pages 681-686, ISSN 0006-291X, https://doi.org/10.1016/j.bbrc.2020.02.119

Functional homo- and heterodimeric actin capping proteins from the malaria parasite

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Author: Bendes, Ábris Ádám1; Chatterjee, Moon2; Götte, Benjamin2;
Organizations: 1Biocenter Oulu and Faculty of Biochemistry and Molecular Medicine, University of Oulu, P.O. Box 5400, 90014, Oulu, Finland
2Centre for Structural Systems Biology, Helmholtz Centre for Infection Research and DESY, Notkestrasse 85, 22607, Hamburg, Germany
3Department of Biomedicine, University of Bergen, Jonas Lies vei 91, Bergen, 5009, Norway
Format: article
Version: accepted version
Access: open
Online Access: PDF Full Text (PDF, 0.9 MB)
Persistent link: http://urn.fi/urn:nbn:fi-fe2020071047232
Language: English
Published: Elsevier, 2020
Publish Date: 2021-03-02
Description:

Abstract

Actin capping proteins belong to the core set of proteins minimally required for actin-based motility and are present in virtually all eukaryotic cells. They bind to the fast-growing barbed end of an actin filament, preventing addition and loss of monomers, thus restricting growth to the slow-growing pointed end. Actin capping proteins are usually heterodimers of two subunits. The Plasmodium orthologs are an exception, as their α subunits are able to form homodimers. We show here that, while the β subunit alone is unstable, the α subunit of the Plasmodium actin capping protein forms functional homo- and heterodimers. This implies independent functions for the αα homo- and αβ heterodimers in certain stages of the parasite life cycle. Structurally, the homodimers resemble canonical αβ heterodimers, although certain rearrangements at the interface must be required. Both homo- and heterodimers bind to actin filaments in a roughly equimolar ratio, indicating they may also bind other sites than barbed ends.

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Series: Biochemical and biophysical research communications
ISSN: 0006-291X
ISSN-E: 1090-2104
ISSN-L: 0006-291X
Volume: 525
Issue: 3
Pages: 681 - 686
DOI: 10.1016/j.bbrc.2020.02.119
OADOI: https://oadoi.org/10.1016/j.bbrc.2020.02.119
Type of Publication: A1 Journal article – refereed
Field of Science: 3111 Biomedicine
Subjects:
Funding: This work was supported by the Academy of Finland, the Sigrid Jusélius Foundation, the Norwegian Research Council, and the German Federal Ministry of Education and Research.
Copyright information: © 2020 Elsevier B.V. This manuscript version is made available under the CC-BY-NC-ND 4.0 license by http://creativecommons.org/licenses/by-nc-nd/4.0/.
  https://creativecommons.org/licenses/by-nc-nd/4.0/