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Structure and function of Plasmodium actin II in the parasite mosquito stages
Actins are filament-forming, highly-conserved proteins in eukaryotes. They are involved in essential processes in the cytoplasm and also have nuclear functions. Malaria parasites (Plasmodium spp.) have two actin isoforms that differ from each other and from canonical actins in structure and filament...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10019781/ https://www.ncbi.nlm.nih.gov/pubmed/36877739 http://dx.doi.org/10.1371/journal.ppat.1011174 |
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author | Lopez, Andrea J. Andreadaki, Maria Vahokoski, Juha Deligianni, Elena Calder, Lesley J. Camerini, Serena Freitag, Anika Bergmann, Ulrich Rosenthal, Peter B. Sidén-Kiamos, Inga Kursula, Inari |
author_facet | Lopez, Andrea J. Andreadaki, Maria Vahokoski, Juha Deligianni, Elena Calder, Lesley J. Camerini, Serena Freitag, Anika Bergmann, Ulrich Rosenthal, Peter B. Sidén-Kiamos, Inga Kursula, Inari |
author_sort | Lopez, Andrea J. |
collection | PubMed |
description | Actins are filament-forming, highly-conserved proteins in eukaryotes. They are involved in essential processes in the cytoplasm and also have nuclear functions. Malaria parasites (Plasmodium spp.) have two actin isoforms that differ from each other and from canonical actins in structure and filament-forming properties. Actin I has an essential role in motility and is fairly well characterized. The structure and function of actin II are not as well understood, but mutational analyses have revealed two essential functions in male gametogenesis and in the oocyst. Here, we present expression analysis, high-resolution filament structures, and biochemical characterization of Plasmodium actin II. We confirm expression in male gametocytes and zygotes and show that actin II is associated with the nucleus in both stages in filament-like structures. Unlike actin I, actin II readily forms long filaments in vitro, and near-atomic structures in the presence or absence of jasplakinolide reveal very similar structures. Small but significant differences compared to other actins in the openness and twist, the active site, the D-loop, and the plug region contribute to filament stability. The function of actin II was investigated through mutational analysis, suggesting that long and stable filaments are necessary for male gametogenesis, while a second function in the oocyst stage also requires fine-tuned regulation by methylation of histidine 73. Actin II polymerizes via the classical nucleation-elongation mechanism and has a critical concentration of ~0.1 μM at the steady-state, like actin I and canonical actins. Similarly to actin I, dimers are a stable form of actin II at equilibrium. |
format | Online Article Text |
id | pubmed-10019781 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-100197812023-03-17 Structure and function of Plasmodium actin II in the parasite mosquito stages Lopez, Andrea J. Andreadaki, Maria Vahokoski, Juha Deligianni, Elena Calder, Lesley J. Camerini, Serena Freitag, Anika Bergmann, Ulrich Rosenthal, Peter B. Sidén-Kiamos, Inga Kursula, Inari PLoS Pathog Research Article Actins are filament-forming, highly-conserved proteins in eukaryotes. They are involved in essential processes in the cytoplasm and also have nuclear functions. Malaria parasites (Plasmodium spp.) have two actin isoforms that differ from each other and from canonical actins in structure and filament-forming properties. Actin I has an essential role in motility and is fairly well characterized. The structure and function of actin II are not as well understood, but mutational analyses have revealed two essential functions in male gametogenesis and in the oocyst. Here, we present expression analysis, high-resolution filament structures, and biochemical characterization of Plasmodium actin II. We confirm expression in male gametocytes and zygotes and show that actin II is associated with the nucleus in both stages in filament-like structures. Unlike actin I, actin II readily forms long filaments in vitro, and near-atomic structures in the presence or absence of jasplakinolide reveal very similar structures. Small but significant differences compared to other actins in the openness and twist, the active site, the D-loop, and the plug region contribute to filament stability. The function of actin II was investigated through mutational analysis, suggesting that long and stable filaments are necessary for male gametogenesis, while a second function in the oocyst stage also requires fine-tuned regulation by methylation of histidine 73. Actin II polymerizes via the classical nucleation-elongation mechanism and has a critical concentration of ~0.1 μM at the steady-state, like actin I and canonical actins. Similarly to actin I, dimers are a stable form of actin II at equilibrium. Public Library of Science 2023-03-06 /pmc/articles/PMC10019781/ /pubmed/36877739 http://dx.doi.org/10.1371/journal.ppat.1011174 Text en © 2023 Lopez et al https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Lopez, Andrea J. Andreadaki, Maria Vahokoski, Juha Deligianni, Elena Calder, Lesley J. Camerini, Serena Freitag, Anika Bergmann, Ulrich Rosenthal, Peter B. Sidén-Kiamos, Inga Kursula, Inari Structure and function of Plasmodium actin II in the parasite mosquito stages |
title | Structure and function of Plasmodium actin II in the parasite mosquito stages |
title_full | Structure and function of Plasmodium actin II in the parasite mosquito stages |
title_fullStr | Structure and function of Plasmodium actin II in the parasite mosquito stages |
title_full_unstemmed | Structure and function of Plasmodium actin II in the parasite mosquito stages |
title_short | Structure and function of Plasmodium actin II in the parasite mosquito stages |
title_sort | structure and function of plasmodium actin ii in the parasite mosquito stages |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10019781/ https://www.ncbi.nlm.nih.gov/pubmed/36877739 http://dx.doi.org/10.1371/journal.ppat.1011174 |
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