Structural Differences Explain Diverse Functions of Plasmodium Actins
Publication Date
April 17, 2014
Journal
PLOS Pathogens
Authors
Juha Vahokoski, Saligram Prabhakar Bhargav, Ambroise Desfosses, Maria Andreadaki, et al
Volume
10
Issue
4
Pages
e1004091
DOI
https://dx.plos.org/10.1371/journal.ppat.1004091
Publisher URL
http://journals.plos.org/plospathogens/article?id=10.1371%2Fjournal.ppat.1004091
PubMed
http://www.ncbi.nlm.nih.gov/pubmed/24743229
PubMed Central
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3990709
Europe PMC
http://europepmc.org/abstract/MED/24743229
Web of Science
000342033600042
Scopus
84901340767
Mendeley
http://www.mendeley.com/research/structural-differences-explain-diverse-functions-plasmodium-actins
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Mendeley | Further Information

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Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/1468175"], "description"=>"<p>(<b>A</b>) In the absence of stabilizing agents, actin I forms only short structures lacking helical symmetry. (<b>B,C</b>) Actin II readily forms filaments varying from hundreds of nm to 1–2 µm in length. (<b>D,E</b>) In the presence of JAS, both parasite actins form long helical filaments. (<b>F</b>) Length distributions of two <i>Plasmodium</i> actin isoforms and three actin I mutants. Note the logarithmic scale of the Y axis.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Cytoskeletal proteins", "Protein interactions", "protein structure", "Protein chemistry", "biophysics", "cell biology", "Cell motility", "Actin filaments", "Molecular cell biology", "molecular biology", "Molecular complexes", "micrographs", "actin"], "article_id"=>1002336, "categories"=>["Biological Sciences"], "users"=>["Juha Vahokoski", "Saligram Prabhakar Bhargav", "Ambroise Desfosses", "Maria Andreadaki", "Esa-Pekka Kumpula", "Silvia Muñico Martinez", "Alexander Ignatev", "Simone Lepper", "Friedrich Frischknecht", "Inga Siden-Kiamos", "Carsten Sachse", "Inari Kursula"], "doi"=>["https://dx.doi.org/10.1371/journal.ppat.1004091.g001"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Electron_micrographs_of_Plasmodium_actin_filaments_/1002336", "title"=>"Electron micrographs of <i>Plasmodium</i> actin filaments.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-04-17 02:56:43"}
  • {"files"=>["https://ndownloader.figshare.com/files/1468183"], "description"=>"<p>(<b>A</b>) Electron cryo-micrographs of actin I and II (left and right, respectively). Side-by-side average power spectrum of actin I and II. (<b>B</b>) Representative class averages from k-means clustering. Center: Histograms of measured cross-over distances reveal a larger half pitch for actin I. (<b>C</b>) Eigen images 1–2 from actin I and II k-means clustering reveal a constant pitch of the one-start helix, whereas Eigen images 3–4 confirm the difference in cross-over distance of actin I and II.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Cytoskeletal proteins", "Protein interactions", "protein structure", "Protein chemistry", "biophysics", "cell biology", "Cell motility", "Actin filaments", "Molecular cell biology", "molecular biology", "Molecular complexes", "actin"], "article_id"=>1002344, "categories"=>["Biological Sciences"], "users"=>["Juha Vahokoski", "Saligram Prabhakar Bhargav", "Ambroise Desfosses", "Maria Andreadaki", "Esa-Pekka Kumpula", "Silvia Muñico Martinez", "Alexander Ignatev", "Simone Lepper", "Friedrich Frischknecht", "Inga Siden-Kiamos", "Carsten Sachse", "Inari Kursula"], "doi"=>["https://dx.doi.org/10.1371/journal.ppat.1004091.g002"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Cryo_EM_image_analysis_of_actin_I_and_II_/1002344", "title"=>"Cryo-EM image analysis of actin I and II.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-04-17 02:56:43"}
  • {"files"=>["https://ndownloader.figshare.com/files/1468185"], "description"=>"<p>(<b>A</b>) The cryo-EM structure of actin I filament at 25 Å resolution (left) in comparison with rabbit skeletal muscle α-actin filtered to a comparable resolution (right; EM database entry EMD-5168 <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1004091#ppat.1004091-Fujii1\" target=\"_blank\">[28]</a>). (<b>B</b>) Symmetry refinement of actin I confirms that the change in cross-over distance is caused mainly by a change in helical rotation when compared with actin II and canonical rabbit α-actin. (<b>C</b>) Fourier Shell correlation of actin I half data sets used for 3D reconstruction. The resolution can be estimated at 25 Å based on the 0.5 criterion.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Cytoskeletal proteins", "Protein interactions", "protein structure", "Protein chemistry", "biophysics", "cell biology", "Cell motility", "Actin filaments", "Molecular cell biology", "molecular biology", "Molecular complexes", "actin", "compared"], "article_id"=>1002346, "categories"=>["Biological Sciences"], "users"=>["Juha Vahokoski", "Saligram Prabhakar Bhargav", "Ambroise Desfosses", "Maria Andreadaki", "Esa-Pekka Kumpula", "Silvia Muñico Martinez", "Alexander Ignatev", "Simone Lepper", "Friedrich Frischknecht", "Inga Siden-Kiamos", "Carsten Sachse", "Inari Kursula"], "doi"=>["https://dx.doi.org/10.1371/journal.ppat.1004091.g003"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Filament_structure_of_Plasmodium_actin_I_compared_to_actin_/1002346", "title"=>"Filament structure of <i>Plasmodium</i> actin I compared to α-actin.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-04-17 02:56:43"}
  • {"files"=>["https://ndownloader.figshare.com/files/1468188"], "description"=>"<p>(<b>A</b>) <i>P. berghei</i> actin II (<i>Pb</i>ActII; yellow) superimposed on α-actin (1eqy <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1004091#ppat.1004091-McLaughlin1\" target=\"_blank\">[39]</a>; cyan). (<b>B</b>) <i>P. falciparum</i> actin I (<i>Pf</i>ActI; red) superimposed on α-actin. In both (<b>A</b>) and (<b>B</b>), ATP, subdomains 1–4, and several regions discussed in the text are indicated. Both N and C termini reside in subdomain 1; the N terminus is visible at the front, and the C-terminal helix is on the back side. Note that the C-terminal helix is not visible in actin I. The C-terminal part and the nearby hydrophobic cluster with Trp357 are shown in the zoomed view on the right and the region involved in intra-filament contacts in subdomain 3 in the box at the lower left corner. The blue and pink dots in (<b>B</b>) indicate the approximate positions of the structural elements shown in detail in (<b>C</b>) and (<b>D</b>), respectively. (<b>C</b>) Lys 207 and Glu188 are at an intimate distance in actin I. A similar salt bridge is present between the corresponding residues in latrunculin-bound α-actin, but the hydrogen-bonding distance is longer without the drug. (<b>D</b>) The proline-rich loop with Gly115 in actin I superimposed on that of α-actin. Note the bending of the loop in actin I, due to the more flexible glycine residue.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Cytoskeletal proteins", "Protein interactions", "protein structure", "Protein chemistry", "biophysics", "cell biology", "Cell motility", "Actin filaments", "Molecular cell biology", "molecular biology", "Molecular complexes", "structures", "actin"], "article_id"=>1002348, "categories"=>["Biological Sciences"], "users"=>["Juha Vahokoski", "Saligram Prabhakar Bhargav", "Ambroise Desfosses", "Maria Andreadaki", "Esa-Pekka Kumpula", "Silvia Muñico Martinez", "Alexander Ignatev", "Simone Lepper", "Friedrich Frischknecht", "Inga Siden-Kiamos", "Carsten Sachse", "Inari Kursula"], "doi"=>["https://dx.doi.org/10.1371/journal.ppat.1004091.g004"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Crystal_structures_of_Plasmodium_actin_I_and_II_/1002348", "title"=>"Crystal structures of <i>Plasmodium</i> actin I and II.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-04-17 02:56:43"}
  • {"files"=>["https://ndownloader.figshare.com/files/1468190"], "description"=>"<p>(<b>A</b>) Electron cryo-micrograph of the chimera filaments. (<b>B</b>) Negatively stained chimera filaments. (<b>C</b>) The crystal structure of the chimera (blue) resembles that of wild-type actin I (red). The zoomed views show the differences in the D-loop around Tyr54 (above) and the C-terminal helix and the hydrophobic residues nearby, which are in the canonical orientation in the chimera, unlike in actin I (below).</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Cytoskeletal proteins", "Protein interactions", "protein structure", "Protein chemistry", "biophysics", "cell biology", "Cell motility", "Actin filaments", "Molecular cell biology", "molecular biology", "Molecular complexes", "actin", "chimera", "forms"], "article_id"=>1002350, "categories"=>["Biological Sciences"], "users"=>["Juha Vahokoski", "Saligram Prabhakar Bhargav", "Ambroise Desfosses", "Maria Andreadaki", "Esa-Pekka Kumpula", "Silvia Muñico Martinez", "Alexander Ignatev", "Simone Lepper", "Friedrich Frischknecht", "Inga Siden-Kiamos", "Carsten Sachse", "Inari Kursula"], "doi"=>["https://dx.doi.org/10.1371/journal.ppat.1004091.g005"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Plasmodium_actin_I_actin_chimera_forms_long_filaments_/1002350", "title"=>"<i>Plasmodium</i> actin I–α-actin chimera forms long filaments.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-04-17 02:56:43"}
  • {"files"=>["https://ndownloader.figshare.com/files/1468193"], "description"=>"<p>(<b>A</b>) The Asn17 side chain in actin I is part of a cluster formed by the Asn17 Nδ and main chain N atoms as well as Nζ of Lys19. Together, they could form an oxyanion hole for stabilizing a negative charge on one of the β-phosphate oxygen atoms in a reaction intermediate. (<b>B</b>) The active-site water structure in actin I is conserved, and W39 is in an almost inline position for a nucleophilic attack to the ATP γ-phosphate. (<b>C</b>) The catalytic water in actin II has moved further away from the ATP γ-phosphate, is mobile, and is likely a double conformation of the water bound directly to His161. (<b>D</b>) Phosphate release rates of the wild-type <i>Plasmodium</i> actins in the calcium- or magnesium-bound states compared to α-actin, the actin I–α-actin chimera and the actin I mutants F54Y and G115A. Error bars represent standard deviation (n = 3).</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Cytoskeletal proteins", "Protein interactions", "protein structure", "Protein chemistry", "biophysics", "cell biology", "Cell motility", "Actin filaments", "Molecular cell biology", "molecular biology", "Molecular complexes", "binding", "sites", "actin"], "article_id"=>1002353, "categories"=>["Biological Sciences"], "users"=>["Juha Vahokoski", "Saligram Prabhakar Bhargav", "Ambroise Desfosses", "Maria Andreadaki", "Esa-Pekka Kumpula", "Silvia Muñico Martinez", "Alexander Ignatev", "Simone Lepper", "Friedrich Frischknecht", "Inga Siden-Kiamos", "Carsten Sachse", "Inari Kursula"], "doi"=>["https://dx.doi.org/10.1371/journal.ppat.1004091.g006"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_ATP_binding_sites_of_actin_I_and_II_/1002353", "title"=>"ATP binding sites of actin I and II.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-04-17 02:56:43"}
  • {"files"=>["https://ndownloader.figshare.com/files/1468194"], "description"=>"<p>(<b>A</b>) <i>Plasmodium</i> actins I (lanes 1–4 and 9) and II (lanes 5–8 and 10) form small oligomers upon storage and after exchange of ATP to ADP. Both parasite actins were studied by native PAGE immediately and 48 h after purification in both ATP and ADP forms. Treatment of ADP-exchanged <i>Plasmodium</i> actins with a high concentration of reducing agent (10 mM TCEP) has no effect on the behavior of either of the actins. Exchange of ATP to ADP in α-actin (lanes 11–14) does not result in changes in the oligomeric state. Nt denotes the nucleotide. TCEP - and + denote either the normal 1 mM or an excessive 10 mM concentration, respectively. The approximate position of the different oligomers, corresponding to lane 2, are given on the left. Note that actin I and II run slightly differently on the gel. (<b>B–F</b>) The relative mobility <i>vs.</i> log MW (circles with the oligomeric state indicated on the side) and relative intensities of bands (bars) extracted from gel images of Coomassie-stained native PAGE gels containing ATP or ADP <i>Plasmodium</i> actin I (<b>B–D</b>) and ADP actin II (<b>E and F</b>) immediately or 48 h after purification. The dark grey bars denote the relative intensity of the bands compared to the most intense band and the light grey bars the relative intensity of the bands compared to the sum of all band intensities.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Cytoskeletal proteins", "Protein interactions", "protein structure", "Protein chemistry", "biophysics", "cell biology", "Cell motility", "Actin filaments", "Molecular cell biology", "molecular biology", "Molecular complexes", "actins"], "article_id"=>1002354, "categories"=>["Biological Sciences"], "users"=>["Juha Vahokoski", "Saligram Prabhakar Bhargav", "Ambroise Desfosses", "Maria Andreadaki", "Esa-Pekka Kumpula", "Silvia Muñico Martinez", "Alexander Ignatev", "Simone Lepper", "Friedrich Frischknecht", "Inga Siden-Kiamos", "Carsten Sachse", "Inari Kursula"], "doi"=>["https://dx.doi.org/10.1371/journal.ppat.1004091.g007"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Native_PAGE_analysis_of_the_Plasmodium_actins_and_actin_/1002354", "title"=>"Native PAGE analysis of the <i>Plasmodium</i> actins and α-actin.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-04-17 02:56:43"}
  • {"files"=>["https://ndownloader.figshare.com/files/1468196"], "description"=>"<p>(<b>A</b>) Exflagellation of a male gametocyte. The residual <i>P. berghei</i> gametocyte is indicated with an asterisk. The flagellar male gametes beat rapidly. The picture is the first frame of <b><a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1004091#ppat.1004091.s008\" target=\"_blank\">Video S1</a></b>. (<b>B</b>) Schematic picture of the <i>actin2</i> gene in wild-type parasites, the recipient strain <i>act2<sup>−</sup>::mCherry</i>, and the final genotypes of the <i>act2com</i>, <i>act2rep</i>, and <i>act1chi</i> strains. The same experimental strategy was used for all constructs. The <i>act1chi</i> strain expresses a chimeric actin, where the D-loop (amino acids 39–61) has been swapped with the D-loop of α-actin (<b>C</b>) Exflagellation assays comparing wild-type (n = 11), <i>act2com</i> (n = 11), <i>act2rep</i> (n = 15) and <i>act1chi</i> (n = 14) parasites. The <i>act2com</i> functionally complemented the mutant, resulting in almost wild-type levels of exflagellation. The <i>act2rep</i> parasites had a significantly smaller number of exflagellation events, while swapping the D-loop of actin I with that of α-actin in the <i>act1chi</i> mutant results in significant restoration of exflagellation. n.s. means non significant, *** stands for P<0.0001, * for P<0.05 (Student's t-test).</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Cytoskeletal proteins", "Protein interactions", "protein structure", "Protein chemistry", "biophysics", "cell biology", "Cell motility", "Actin filaments", "Molecular cell biology", "molecular biology", "Molecular complexes", "d-loop", "chimera", "wild-type", "actin", "rescues", "phenotype", "deletion"], "article_id"=>1002356, "categories"=>["Biological Sciences"], "users"=>["Juha Vahokoski", "Saligram Prabhakar Bhargav", "Ambroise Desfosses", "Maria Andreadaki", "Esa-Pekka Kumpula", "Silvia Muñico Martinez", "Alexander Ignatev", "Simone Lepper", "Friedrich Frischknecht", "Inga Siden-Kiamos", "Carsten Sachse", "Inari Kursula"], "doi"=>["https://dx.doi.org/10.1371/journal.ppat.1004091.g008"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_D_loop_chimera_but_not_wild_type_actin_I_rescues_the_phenotype_of_the_actin2_deletion_mutant_/1002356", "title"=>"The D-loop chimera but not wild-type actin I rescues the phenotype of the <i>actin2</i> deletion mutant.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-04-17 02:56:43"}
  • {"files"=>["https://ndownloader.figshare.com/files/1468197"], "description"=>"<p>*Values in parentheses are for the highest-resolution shell.</p>#<p>R<sub>meas</sub> is the redundancy-independent <i>R</i> factor <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1004091#ppat.1004091-Diederichs1\" target=\"_blank\">[94]</a>, <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1004091#ppat.1004091-Weiss1\" target=\"_blank\">[95]</a>.</p>†<p>CC<sub>1/2</sub> is defined as the correlation coefficient between two random half data sets <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1004091#ppat.1004091-Karplus1\" target=\"_blank\">[96]</a>.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Cytoskeletal proteins", "Protein interactions", "protein structure", "Protein chemistry", "biophysics", "cell biology", "Cell motility", "Actin filaments", "Molecular cell biology", "molecular biology", "Molecular complexes", "refinement"], "article_id"=>1002357, "categories"=>["Biological Sciences"], "users"=>["Juha Vahokoski", "Saligram Prabhakar Bhargav", "Ambroise Desfosses", "Maria Andreadaki", "Esa-Pekka Kumpula", "Silvia Muñico Martinez", "Alexander Ignatev", "Simone Lepper", "Friedrich Frischknecht", "Inga Siden-Kiamos", "Carsten Sachse", "Inari Kursula"], "doi"=>["https://dx.doi.org/10.1371/journal.ppat.1004091.t001"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Data_collection_and_refinement_statistics_/1002357", "title"=>"Data collection and refinement statistics.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2014-04-17 02:56:43"}
  • {"files"=>["https://ndownloader.figshare.com/files/1468227", "https://ndownloader.figshare.com/files/1468228", "https://ndownloader.figshare.com/files/1468229", "https://ndownloader.figshare.com/files/1468230", "https://ndownloader.figshare.com/files/1468231", "https://ndownloader.figshare.com/files/1468232", "https://ndownloader.figshare.com/files/1468233", "https://ndownloader.figshare.com/files/1468234"], "description"=>"<div><p>Actins are highly conserved proteins and key players in central processes in all eukaryotic cells. The two actins of the malaria parasite are among the most divergent eukaryotic actins and also differ from each other more than isoforms in any other species. Microfilaments have not been directly observed in <i>Plasmodium</i> and are presumed to be short and highly dynamic. We show that actin I cannot complement actin II in male gametogenesis, suggesting critical structural differences. Cryo-EM reveals that <i>Plasmodium</i> actin I has a unique filament structure, whereas actin II filaments resemble canonical F-actin. Both <i>Plasmodium</i> actins hydrolyze ATP more efficiently than α-actin, and unlike any other actin, both parasite actins rapidly form short oligomers induced by ADP. Crystal structures of both isoforms pinpoint several structural changes in the monomers causing the unique polymerization properties. Inserting the canonical D-loop to <i>Plasmodium</i> actin I leads to the formation of long filaments <i>in vitro</i>. <i>In vivo</i>, this chimera restores gametogenesis in parasites lacking actin II, suggesting that stable filaments are required for exflagellation. Together, these data underline the divergence of eukaryotic actins and demonstrate how structural differences in the monomers translate into filaments with different properties, implying that even eukaryotic actins have faced different evolutionary pressures and followed different paths for developing their polymerization properties.</p></div>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Cytoskeletal proteins", "Protein interactions", "protein structure", "Protein chemistry", "biophysics", "cell biology", "Cell motility", "Actin filaments", "Molecular cell biology", "molecular biology", "Molecular complexes", "differences", "functions", "actins"], "article_id"=>1002376, "categories"=>["Biological Sciences"], "users"=>["Juha Vahokoski", "Saligram Prabhakar Bhargav", "Ambroise Desfosses", "Maria Andreadaki", "Esa-Pekka Kumpula", "Silvia Muñico Martinez", "Alexander Ignatev", "Simone Lepper", "Friedrich Frischknecht", "Inga Siden-Kiamos", "Carsten Sachse", "Inari Kursula"], "doi"=>["https://dx.doi.org/10.1371/journal.ppat.1004091.s001", "https://dx.doi.org/10.1371/journal.ppat.1004091.s002", "https://dx.doi.org/10.1371/journal.ppat.1004091.s003", "https://dx.doi.org/10.1371/journal.ppat.1004091.s004", "https://dx.doi.org/10.1371/journal.ppat.1004091.s005", "https://dx.doi.org/10.1371/journal.ppat.1004091.s006", "https://dx.doi.org/10.1371/journal.ppat.1004091.s007", "https://dx.doi.org/10.1371/journal.ppat.1004091.s008"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Structural_Differences_Explain_Diverse_Functions_of_Plasmodium_Actins/1002376", "title"=>"Structural Differences Explain Diverse Functions of <i>Plasmodium</i> Actins", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2014-04-17 02:56:43"}

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