A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
Functional homo- and heterodimeric actin capping proteins from the malaria parasite
Tekijät: Bendes Ábris Ádám, Chatterjee Moon, Gotte Benjamin, Kursula Petri, Kursula Inari
Kustantaja: ACADEMIC PRESS INC ELSEVIER SCIENCE
Julkaisuvuosi: 2020
Journal: Biochemical and Biophysical Research Communications
Tietokannassa oleva lehden nimi: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Lehden akronyymi: BIOCHEM BIOPH RES CO
Vuosikerta: 525
Numero: 3
Aloitussivu: 681
Lopetussivu: 686
Sivujen määrä: 6
ISSN: 0006-291X
DOI: https://doi.org/10.1016/j.bbrc.2020.02.119
Tiivistelmä
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 a subunits are able to form homodimers. We show here that, while the beta subunit alone is unstable, the alpha subunit of the Plasmodium actin capping protein forms functional homo- and heterodimers. This implies independent functions for the alpha alpha homo- and alpha beta heterodimers in certain stages of the parasite life cycle. Structurally, the homodimers resemble canonical alpha beta 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. (C) 2020 Published by Elsevier Inc.
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 a subunits are able to form homodimers. We show here that, while the beta subunit alone is unstable, the alpha subunit of the Plasmodium actin capping protein forms functional homo- and heterodimers. This implies independent functions for the alpha alpha homo- and alpha beta heterodimers in certain stages of the parasite life cycle. Structurally, the homodimers resemble canonical alpha beta 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. (C) 2020 Published by Elsevier Inc.
Turun yliopiston Tutkimustietojärjestelmän portaali