Identification of O-mannosylated Virulence Factors in Ustilago maydis
Publication Date
March 01, 2012
Journal
PLOS Pathogens
Authors
Alfonso Fernández Álvarez, Miriam Marín Menguiano, Daniel Lanver, Alberto Jiménez Martín, et al
Volume
8
Issue
3
Pages
e1002563
DOI
http://doi.org/10.1371/journal.ppat.1002563
Publisher URL
http://journals.plos.org/plospathogens/article?id=10.1371%2Fjournal.ppat.1002563
PubMed
http://www.ncbi.nlm.nih.gov/pubmed/22416226
PubMed Central
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3295589
Europe PMC
http://europepmc.org/abstract/MED/22416226
Web of Science
000302225600017
Scopus
84863570532
Mendeley
http://www.mendeley.com/research/identification-omannosylated-virulence-factors-ustilago-maydis
Events
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Mendeley | Further Information

{"title"=>"Identification of O-mannosylated virulence factors in Ustilago maydis.", "type"=>"journal", "authors"=>[{"first_name"=>"Alfonso", "last_name"=>"Fernández-Álvarez", "scopus_author_id"=>"35749841200"}, {"first_name"=>"Miriam", "last_name"=>"Marín-Menguiano", "scopus_author_id"=>"55303748700"}, {"first_name"=>"Daniel", "last_name"=>"Lanver", "scopus_author_id"=>"36440080300"}, {"first_name"=>"Alberto", "last_name"=>"Jiménez-Martín", "scopus_author_id"=>"55303713200"}, {"first_name"=>"Alberto", "last_name"=>"Elías-Villalobos", "scopus_author_id"=>"35749851700"}, {"first_name"=>"Antonio J.", "last_name"=>"Pérez-Pulido", "scopus_author_id"=>"36158431100"}, {"first_name"=>"Regine", "last_name"=>"Kahmann", "scopus_author_id"=>"7005538520"}, {"first_name"=>"José I.", "last_name"=>"Ibeas", "scopus_author_id"=>"6603363412"}], "year"=>2012, "source"=>"PLoS pathogens", "identifiers"=>{"scopus"=>"2-s2.0-84863570532", "pui"=>"365183996", "sgr"=>"84863570532", "pmid"=>"22416226", "issn"=>"15537374", "doi"=>"10.1371/journal.ppat.1002563", "isbn"=>"1553-7374 (Electronic)\\r1553-7366 (Linking)"}, "id"=>"77736f4c-65cf-38df-92f5-c6dd44510277", "abstract"=>"The O-mannosyltransferase Pmt4 has emerged as crucial for fungal virulence in the animal pathogens Candida albicans or Cryptococcus neoformans as well as in the phytopathogenic fungus Ustilago maydis. Pmt4 O-mannosylates specific target proteins at the Endoplasmic Reticulum. Therefore a deficient O-mannosylation of these target proteins must be responsible for the loss of pathogenicity in pmt4 mutants. Taking advantage of the characteristics described for Pmt4 substrates in Saccharomyces cerevisiae, we performed a proteome-wide bioinformatic approach to identify putative Pmt4 targets in the corn smut fungus U. maydis and validated Pmt4-mediated glycosylation of candidate proteins by electrophoretic mobility shift assays. We found that the signalling mucin Msb2, which regulates appressorium differentiation upstream of the pathogenicity-related MAP kinase cascade, is O-mannosylated by Pmt4. The epistatic relationship of pmt4 and msb2 showed that both are likely to act in the same pathway. Furthermore, constitutive activation of the MAP kinase cascade restored appressorium development in pmt4 mutants, suggesting that during the initial phase of infection the failure to O-mannosylate Msb2 is responsible for the virulence defect of pmt4 mutants. On the other hand we demonstrate that during later stages of pathogenic development Pmt4 affects virulence independently of Msb2, probably by modifying secreted effector proteins. Pit1, a protein required for fungal spreading inside the infected leaf, was also identified as a Pmt4 target. Thus, O-mannosylation of different target proteins affects various stages of pathogenic development in U. maydis.", "link"=>"http://www.mendeley.com/research/identification-omannosylated-virulence-factors-ustilago-maydis", "reader_count"=>34, "reader_count_by_academic_status"=>{"Professor > Associate Professor"=>2, "Researcher"=>5, "Student > Doctoral Student"=>5, "Student > Ph. D. Student"=>5, "Student > Postgraduate"=>1, "Student > Master"=>11, "Student > Bachelor"=>3, "Lecturer"=>1, "Professor"=>1}, "reader_count_by_user_role"=>{"Professor > Associate Professor"=>2, "Researcher"=>5, "Student > Doctoral Student"=>5, "Student > Ph. D. Student"=>5, "Student > Postgraduate"=>1, "Student > Master"=>11, "Student > Bachelor"=>3, "Lecturer"=>1, "Professor"=>1}, "reader_count_by_subject_area"=>{"Environmental Science"=>1, "Biochemistry, Genetics and Molecular Biology"=>8, "Agricultural and Biological Sciences"=>24, "Medicine and Dentistry"=>1}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>24}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>8}, "Environmental Science"=>{"Environmental Science"=>1}}, "reader_count_by_country"=>{"Chile"=>1, "Spain"=>1}, "group_count"=>0}

CrossRef

Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/675565"], "description"=>"<p><b>A.</b> Seven day old maize seedlings were infected with the strains SG200 (WT), SG200fuz7DD, SG200Δpmt4 and SG200fuz7DDΔpmt4. Appressoria production was scored 15 hours later quantifying >100 filaments in each case. Data are shown as mean values ±SEM. Asterisk indicates statistically significant differences between wild-type (control) and Δpmt4 strains, P value≤0.001. <b>B.</b> Plant penetration was evaluated quantifying appressoria penetration versus appressoria on plant leaves stained with chlorazol black two days after infection. The quantification was performed with the strains indicated. Data represent the mean values ±SEM. The number of appressoria analysed in each case was ≥50. Asterisk indicates statistically significant differences between wild-type (control) and Δpmt4 strains (P value≤0.001). <b>C.</b> Appressorium penetration is normal in the SG200fuz7DDΔpmt4 strain. The <i>z</i> axis image projections show the site of penetration (0 µm) and the hyphae invading into plant cells (−15 µm). Δpmt4 strain is the only one unable to penetrate the plant cuticle. <b>D.</b> Infected leaves were stained with chlorazol black two days after inoculation. Hyphae of the solopathogenic strains SG200 (WT), SG200fuz7DD and SG200fuz7DDΔpmt4 form clamp-like structures <i>in planta</i> (framed in red). However clamp-like structures are not observed in SG200Δpmt4 infections only recognize appressorium formation on the plant surface. Bar represents 20 µm.</p>", "links"=>[], "tags"=>["hyperactive", "allele", "rescues", "appressorium", "penetration", "defects"], "article_id"=>346036, "categories"=>["Microbiology"], "users"=>["Alfonso Fernández-Álvarez", "Miriam Marín-Menguiano", "Daniel Lanver", "Alberto Jiménez-Martín", "Alberto Elías-Villalobos", "Antonio J. Pérez-Pulido", "Regine Kahmann", "José I. Ibeas"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1002563.g005", "stats"=>{"downloads"=>3, "page_views"=>22, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_hyperactive_allele_fuz7DD_rescues_the_appressorium_formation_and_penetration_defects_of_the_pmt4_strain_/346036", "title"=>"The hyperactive allele <i>fuz7DD</i> rescues the appressorium formation and penetration defects of the Δpmt4 strain.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-03-01 01:40:36"}
  • {"files"=>["https://ndownloader.figshare.com/files/676099"], "description"=>"<p>Pmt4 has a major function in appressorium biology: Pmt4 O-mannosylates Msb2, a membrane-sensor that regulates appressorium development upstream of the MAP kinase cascade. The deletion of <i>pmt4</i> severely affects appressorium formation, probably due to a deficient glycosylation of Msb2. During appressorium-mediated penetration Pmt4 also probably acts above the MAP kinase cascade. Furthermore, Pmt4 plays a role <i>in planta</i> by O-mannosylation of proteins required for tumor formation.</p>", "links"=>[], "tags"=>["pmt4", "developed", "pathogenic"], "article_id"=>346586, "categories"=>["Microbiology"], "users"=>["Alfonso Fernández-Álvarez", "Miriam Marín-Menguiano", "Daniel Lanver", "Alberto Jiménez-Martín", "Alberto Elías-Villalobos", "Antonio J. Pérez-Pulido", "Regine Kahmann", "José I. Ibeas"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1002563.g010", "stats"=>{"downloads"=>1, "page_views"=>7, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Model_of_the_Pmt4_roles_developed_during_U_maydis_pathogenic_development_/346586", "title"=>"Model of the Pmt4 roles developed during <i>U. maydis</i> pathogenic development.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-03-01 01:49:46"}
  • {"files"=>["https://ndownloader.figshare.com/files/675682"], "description"=>"<p><b>A.</b> Disease progression in plant infections with the strains indicated. No infection symptoms were detected on plants inoculated with the SG200Δpmt4 strain. The SG200fuz7DDΔpmt4 induces anthocyanin production and small tumors formation. Bar represents 2 cm. <b>B.</b> Plants were infected with the indicated strains and symptoms were scored 12 days post-infection. <i>N</i> indicates the total number of plants evaluated in each case.</p>", "links"=>[], "tags"=>["restores", "induction"], "article_id"=>346165, "categories"=>["Microbiology"], "users"=>["Alfonso Fernández-Álvarez", "Miriam Marín-Menguiano", "Daniel Lanver", "Alberto Jiménez-Martín", "Alberto Elías-Villalobos", "Antonio J. Pérez-Pulido", "Regine Kahmann", "José I. Ibeas"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1002563.g006", "stats"=>{"downloads"=>1, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Expression_of_fuz7DD_in_the_pmt4_strain_partially_restores_the_tumor_induction_in_maize_/346165", "title"=>"Expression of <i>fuz7DD</i> in the Δpmt4 strain partially restores the tumor induction in maize.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-03-01 01:42:45"}
  • {"files"=>["https://ndownloader.figshare.com/files/675889"], "description"=>"<p>The strains indicated FB1 and FB1Δpmt4 were grown to A600 = 0.5 in YEPSL liquid medium and then were spotted on starch medium plates, according to the random distribution scheme shown, and incubated for three days at 28°C. Later, the plate surface was gentle washed. The FB1Δpmt1 strain was used as control of the effect of the loss of other protein O-mannosyltransferase. The deletion of <i>pmt4</i> reduces significantly the fungal cell adhesion to solid surfaces in <i>U. maydis</i>.</p>", "links"=>[], "tags"=>["cellular", "adhesion", "surfaces"], "article_id"=>346371, "categories"=>["Microbiology"], "users"=>["Alfonso Fernández-Álvarez", "Miriam Marín-Menguiano", "Daniel Lanver", "Alberto Jiménez-Martín", "Alberto Elías-Villalobos", "Antonio J. Pérez-Pulido", "Regine Kahmann", "José I. Ibeas"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1002563.g008", "stats"=>{"downloads"=>1, "page_views"=>7, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Pmt4_is_required_for_cellular_adhesion_to_solid_surfaces_in_U_maydis_/346371", "title"=>"Pmt4 is required for cellular adhesion to solid surfaces in <i>U. maydis</i>.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-03-01 01:46:11"}
  • {"files"=>["https://ndownloader.figshare.com/files/675999"], "description"=>"<p><b>A–B.</b> Seven days old maize seedlings were inoculated with SG200 (WT), SG200Δpmt4 and SG200Δpmt4P<sub>otef</sub>:pmt4. To check the appressorium penetration phenotype plant leaves were stained with chlorazol black two days after infection. The <i>z</i> axis image projections show the site of penetration (0 µm) and the hyphae invading into plant cells (−15 µm). <b>C.</b> Quantification of appressorium penetration. Data represent the mean values ±SEM. The number of appressoria analysed in each case was ≥30. <b>D.</b> 12 days after infection anthocyanin production and tumor formation were observed on plants infected with the wild-type while no infection symptoms were detected on plants inoculated with the <i>pmt4</i> mutant strain. The SG200Δpmt4P<sub>otef</sub>:pmt4 induces anthocyanin production and small tumors formation but not prominent tumors which suggest a role of Pmt4 after plant penetration. Bar represents 2 cm. <b>E.</b> Three independent experiments were performed 12 days post-infection and the average values are expressed as a percentage of the total number of infected plants (indicated by <i>N</i>). The strains analysed are shown below each column.</p>", "links"=>[], "tags"=>["fungal", "proliferation"], "article_id"=>346484, "categories"=>["Microbiology"], "users"=>["Alfonso Fernández-Álvarez", "Miriam Marín-Menguiano", "Daniel Lanver", "Alberto Jiménez-Martín", "Alberto Elías-Villalobos", "Antonio J. Pérez-Pulido", "Regine Kahmann", "José I. Ibeas"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1002563.g009", "stats"=>{"downloads"=>1, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Pmt4_plays_a_role_in_the_fungal_proliferation_inside_the_plant_tissues_/346484", "title"=>"Pmt4 plays a role in the fungal proliferation inside the plant tissues.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-03-01 01:48:04"}
  • {"files"=>["https://ndownloader.figshare.com/files/675784"], "description"=>"<p>Crosses of the sexually compatible strains FB1 and FB2, and FB1Δpmt4 and FB2Δpmt4 were inoculated into maize seedlings. Leaves were fixed and analysed by Scanning Electron Microscopy (SEM) one day post infection. In these images (left), we can observe appressorium formation over a plant stomata (pointed with a red arrow) penetrating the plant surface in the wild-type. However, in a similar scenario, with the appressorium developed over plant stomata, the <i>pmt4</i> mutant is unable to penetrate the plant cuticle, producing hyphal outgrowing. This morphologic structure seems to be a consequence of its incapability to penetrate this surface as we can deduce from wild-type phenotype of the <i>in vitro</i> appressorium formation on the non-penetrable surface of parafilm M (right). The <i>in vitro</i> analysis was performed by fluorescence microscopy staining the cells with calcofluor white 15 hours after being sprayed on parafilm M (see <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1002563#s4\" target=\"_blank\">Methods</a> for additional details). Scale bar on the <i>in vitro</i> conditions represents 20 µm.</p>", "links"=>[], "tags"=>["mutant", "appressorium", "shows", "outgrowing", "incapability", "penetrate"], "article_id"=>346257, "categories"=>["Microbiology"], "users"=>["Alfonso Fernández-Álvarez", "Miriam Marín-Menguiano", "Daniel Lanver", "Alberto Jiménez-Martín", "Alberto Elías-Villalobos", "Antonio J. Pérez-Pulido", "Regine Kahmann", "José I. Ibeas"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1002563.g007", "stats"=>{"downloads"=>1, "page_views"=>16, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_pmt4_mutant_appressorium_shows_outgrowing_as_a_consequence_of_its_incapability_to_penetrate_the_plant_cuticle_/346257", "title"=>"The <i>pmt4</i> mutant appressorium shows outgrowing as a consequence of its incapability to penetrate the plant cuticle.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-03-01 01:44:17"}
  • {"files"=>["https://ndownloader.figshare.com/files/344498", "https://ndownloader.figshare.com/files/344529", "https://ndownloader.figshare.com/files/344597", "https://ndownloader.figshare.com/files/344631", "https://ndownloader.figshare.com/files/344666", "https://ndownloader.figshare.com/files/344717", "https://ndownloader.figshare.com/files/344767", "https://ndownloader.figshare.com/files/344816", "https://ndownloader.figshare.com/files/344880", "https://ndownloader.figshare.com/files/344925", "https://ndownloader.figshare.com/files/344941", "https://ndownloader.figshare.com/files/344961", "https://ndownloader.figshare.com/files/344975"], "description"=>"<div><p>The O-mannosyltransferase Pmt4 has emerged as crucial for fungal virulence in the animal pathogens <em>Candida albicans</em> or <em>Cryptococcus neoformans</em> as well as in the phytopathogenic fungus <em>Ustilago maydis</em>. Pmt4 O-mannosylates specific target proteins at the Endoplasmic Reticulum. Therefore a deficient O-mannosylation of these target proteins must be responsible for the loss of pathogenicity in <em>pmt4</em> mutants. Taking advantage of the characteristics described for Pmt4 substrates in <em>Saccharomyces cerevisiae</em>, we performed a proteome-wide bioinformatic approach to identify putative Pmt4 targets in the corn smut fungus <em>U. maydis</em> and validated Pmt4-mediated glycosylation of candidate proteins by electrophoretic mobility shift assays. We found that the signalling mucin Msb2, which regulates appressorium differentiation upstream of the pathogenicity-related MAP kinase cascade, is O-mannosylated by Pmt4. The epistatic relationship of <em>pmt4</em> and <em>msb2</em> showed that both are likely to act in the same pathway. Furthermore, constitutive activation of the MAP kinase cascade restored appressorium development in <em>pmt4</em> mutants, suggesting that during the initial phase of infection the failure to O-mannosylate Msb2 is responsible for the virulence defect of <em>pmt4</em> mutants. On the other hand we demonstrate that during later stages of pathogenic development Pmt4 affects virulence independently of Msb2, probably by modifying secreted effector proteins. Pit1, a protein required for fungal spreading inside the infected leaf, was also identified as a Pmt4 target. Thus, O-mannosylation of different target proteins affects various stages of pathogenic development in <em>U. maydis</em>.</p> </div>", "links"=>[], "tags"=>["o-mannosylated", "virulence", "factors"], "article_id"=>128098, "categories"=>["Microbiology"], "users"=>["Alfonso Fernández-Álvarez", "Miriam Marín-Menguiano", "Daniel Lanver", "Alberto Jiménez-Martín", "Alberto Elías-Villalobos", "Antonio J. Pérez-Pulido", "Regine Kahmann", "José I. Ibeas"], "doi"=>["https://dx.doi.org/10.1371/journal.ppat.1002563.s001", "https://dx.doi.org/10.1371/journal.ppat.1002563.s002", "https://dx.doi.org/10.1371/journal.ppat.1002563.s003", "https://dx.doi.org/10.1371/journal.ppat.1002563.s004", "https://dx.doi.org/10.1371/journal.ppat.1002563.s005", "https://dx.doi.org/10.1371/journal.ppat.1002563.s006", "https://dx.doi.org/10.1371/journal.ppat.1002563.s007", "https://dx.doi.org/10.1371/journal.ppat.1002563.s008", "https://dx.doi.org/10.1371/journal.ppat.1002563.s009", "https://dx.doi.org/10.1371/journal.ppat.1002563.s010", "https://dx.doi.org/10.1371/journal.ppat.1002563.s011", "https://dx.doi.org/10.1371/journal.ppat.1002563.s012", "https://dx.doi.org/10.1371/journal.ppat.1002563.s013"], "stats"=>{"downloads"=>5, "page_views"=>37, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Identification_of_O_mannosylated_Virulence_Factors_in_Ustilago_maydis_/128098", "title"=>"Identification of O-mannosylated Virulence Factors in <em>Ustilago maydis</em>", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2012-03-01 02:14:58"}
  • {"files"=>["https://ndownloader.figshare.com/files/676176"], "description"=>"<p><i>U. maydis</i> strains used in this study.</p>", "links"=>[], "tags"=>["strains"], "article_id"=>346666, "categories"=>["Microbiology"], "users"=>["Alfonso Fernández-Álvarez", "Miriam Marín-Menguiano", "Daniel Lanver", "Alberto Jiménez-Martín", "Alberto Elías-Villalobos", "Antonio J. Pérez-Pulido", "Regine Kahmann", "José I. Ibeas"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1002563.t001", "stats"=>{"downloads"=>1, "page_views"=>2, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_U_maydis_strains_used_in_this_study_/346666", "title"=>"<i>U. maydis</i> strains used in this study.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2012-03-01 01:51:06"}
  • {"files"=>["https://ndownloader.figshare.com/files/675344"], "description"=>"<p><b>A.</b> Schematic model of the protein variant Msb2ΔSTR-GFP compared to Msb2-HA-GFP. The deletion of the coding region of the Ser/Thr rich domain of Msb2 is shown. <b>B.</b> Cells of SG200Δmsb2/msb2-HA-GFP and SG200Δmsb2/msb2ΔSTR-GFP were grown to mid log phase in YEPSL and analyzed microscopically without addition (top row) or after addition of latrunculin A (bottom row). The fluorescent signal corresponding to GFP is shown. <b>C.</b> Total protein extracts of the indicated strains were subjected to western analysis with α-HA antibody (upper panel) and α-GFP antibody (middle panel). Tubulin served as loading control and was detected with α-tubulin antibody (bottom panel). The fusion proteins and processed fragments are indicated by arrowheads on the right. The molecular weight ruler is depicted on the left. <b>D.</b> Disease symptoms caused by SG200 (WT), SG200Δmsb2, and SG200Δmsb2 complemented with either Potef:msb2 or Potef:msb2ΔSTR were scored 12 dpi. <i>N</i> indicates the total number of plants evaluated in each case.</p>", "links"=>[], "tags"=>["str", "msb2"], "article_id"=>345829, "categories"=>["Microbiology"], "users"=>["Alfonso Fernández-Álvarez", "Miriam Marín-Menguiano", "Daniel Lanver", "Alberto Jiménez-Martín", "Alberto Elías-Villalobos", "Antonio J. Pérez-Pulido", "Regine Kahmann", "José I. Ibeas"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1002563.g003", "stats"=>{"downloads"=>1, "page_views"=>14, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_STR_region_is_required_for_Msb2_function_in_U_maydis_/345829", "title"=>"The STR region is required for Msb2 function in <i>U. maydis</i>.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-03-01 01:37:09"}
  • {"files"=>["https://ndownloader.figshare.com/files/675267"], "description"=>"<p><b>A.</b> Domain architecture of the Msb2-HA-GFP fusion protein. The HA-epitope is integrated at amino acid 709 and the C-terminus is fused to GFP. The Ser/Thr rich region as well as the predicted proteolytic cleavage site is indicated. <b>B.</b> Western Blot analysis of Msb2-HA-GFP isolated from SG200Δmsb2/msb2-HA-GFP (WT) and two independent clones of SG200Δmsb2Δpmt4/msb2-HA-GFP (#1 and #2, respectively). SG200 was used as a control. The first gel (above) contains 6% of polyacrylamide and α-HA antibody was used to detect the N-terminal part of Msb2. The other gel (below) contains 10% of polyacrylamide and was treated with α-GFP antibody to detect the C-terminus of Msb2. Equal amounts of proteins of total cell extracts were loaded in each lane.</p>", "links"=>[], "tags"=>["pmt4", "substrate"], "article_id"=>345750, "categories"=>["Microbiology"], "users"=>["Alfonso Fernández-Álvarez", "Miriam Marín-Menguiano", "Daniel Lanver", "Alberto Jiménez-Martín", "Alberto Elías-Villalobos", "Antonio J. Pérez-Pulido", "Regine Kahmann", "José I. Ibeas"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1002563.g002", "stats"=>{"downloads"=>1, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Msb2_is_a_Pmt4_substrate_in_U_maydis_/345750", "title"=>"Msb2 is a Pmt4 substrate in <i>U. maydis</i>.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-03-01 01:35:50"}
  • {"files"=>["https://ndownloader.figshare.com/files/675143"], "description"=>"<p><b>A.</b> In the first step, we selected those proteins containing plasma membrane anchoring and a window of 20 aa where the percentage of Ser/Thr was ≥40%. 826 of the 6787 proteins contained in the <i>U. maydis</i> proteome (MIPS) fulfilled both conditions. In the second stage, we required a wider Ser/Thr rich region, of 40 aa containing a percentage of Ser/Thr ≥40%. We found 306 proteins. Finally, we searched for those containing the Ser/Thr rich region in the luminal part of the protein. With this filter, the list was reduced up to 64 putative Pmt4 target proteins. <b>B.</b> Validation of the <i>in silico</i> screening of Pmt4 target proteins in <i>U. maydis</i>. The figure shows the western blot analysis of Um03746 (∼34 KDa), Um03749 (∼30 KDa), Pit1 (∼48 KDa) and Um04580 (∼36 KDa) proteins tagged with GFP (∼27 KDa) in the SG200 (WT) and SG200Δpmt4 backgrounds. Um03749, Pit1 and Um04580 suffer a differential glycosylation processing in the <i>pmt4</i> mutant since we did not observe the bands that probably correspond to the glycosylated fraction of the proteins. The Um03746 processing does not seem to be affected by the loss of <i>pmt4</i>.</p>", "links"=>[], "tags"=>["validation", "pmt4"], "article_id"=>345622, "categories"=>["Microbiology"], "users"=>["Alfonso Fernández-Álvarez", "Miriam Marín-Menguiano", "Daniel Lanver", "Alberto Jiménez-Martín", "Alberto Elías-Villalobos", "Antonio J. Pérez-Pulido", "Regine Kahmann", "José I. Ibeas"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1002563.g001", "stats"=>{"downloads"=>1, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Design_and_validation_of_the_in_silico_screening_of_Pmt4_target_proteins_/345622", "title"=>"Design and validation of the <i>in silico</i> screening of Pmt4 target proteins.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-03-01 01:33:42"}
  • {"files"=>["https://ndownloader.figshare.com/files/675450"], "description"=>"<p><b>A.</b> Chemical plant-derived signals reception does not depend on Pmt4. SG200 (WT) and its derivative mutants were grown to exponential phase and incubated in liquid medium (2% YEPSL in water) supplemented with 100 µM of 16-hydroxyhexadecanoic acid dissolved in ethanol or ethanol (control) for 18 hours at 28°C. Filament formation was analyzed. All data are shown as mean values ±SEM of three independent repetitions quantifying 200 cells in each case. <b>B.</b> Physical signals reception depends on Pmt4. SG200AM1 (WT) and its derivative mutants were sprayed as cell suspension (2% YEPSL) on parafilm M with or without 100 µM 16-hydroxyhexadecanoic acid and incubated for 18 hours at 28°C. Cells were stained with calcofluor white (CFW) and appressorium formation was scored visualizing the expression of the GFP reporter gene. Appressorium formation was reduced in all analysed mutants. Scale bar represents 50 µm. <b>C.</b> Quantification of appressoria production. The assay was performed as described in B. In three independent experiments, approximately 100 filaments per strain and experiment were analyzed with respect to appressorium formation. All data are shown as mean values ±SEM. Asterisk indicates statistically significant differences between wild-type (control) and each mutant. Single asterisk means P value≤0.001.</p>", "links"=>[], "tags"=>["mutants", "hydroxy", "fatty", "hydrophobic"], "article_id"=>345929, "categories"=>["Microbiology"], "users"=>["Alfonso Fernández-Álvarez", "Miriam Marín-Menguiano", "Daniel Lanver", "Alberto Jiménez-Martín", "Alberto Elías-Villalobos", "Antonio J. Pérez-Pulido", "Regine Kahmann", "José I. Ibeas"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1002563.g004", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_pmt4_and_the_double_msb2_pmt4_mutants_respond_to_hydroxy_fatty_acid_but_not_to_hydrophobic_surfaces_/345929", "title"=>"The <i>pmt4</i> and the double <i>msb2 pmt4</i> mutants respond to hydroxy fatty acid but not to hydrophobic surfaces.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-03-01 01:38:49"}

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Relative Metric

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