Aminoacyl-tRNA-Charged Eukaryotic Elongation Factor 1A Is the Bona Fide Substrate for Legionella pneumophila Effector Glucosyltransferases
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{"title"=>"Aminoacyl-tRNA-charged eukaryotic elongation factor 1A is the bona fide substrate for Legionella pneumophila effector glucosyltransferases", "type"=>"journal", "authors"=>[{"first_name"=>"Tina", "last_name"=>"Tzivelekidis", "scopus_author_id"=>"35219370100"}, {"first_name"=>"Thomas", "last_name"=>"Jank", "scopus_author_id"=>"9274083600"}, {"first_name"=>"Corinna", "last_name"=>"Pohl", "scopus_author_id"=>"37027020400"}, {"first_name"=>"Andreas", "last_name"=>"Schlosser", "scopus_author_id"=>"55621576800"}, {"first_name"=>"Sabine", "last_name"=>"Rospert", "scopus_author_id"=>"7004165921"}, {"first_name"=>"Charlotte R.", "last_name"=>"Knudsen", "scopus_author_id"=>"7006716124"}, {"first_name"=>"Marina V.", "last_name"=>"Rodnina", "scopus_author_id"=>"7006116936"}, {"first_name"=>"Yury", "last_name"=>"Belyi", "scopus_author_id"=>"15061270000"}, {"first_name"=>"Klaus", "last_name"=>"Aktories", "scopus_author_id"=>"7102230719"}], "year"=>2011, "source"=>"PLoS ONE", "identifiers"=>{"issn"=>"19326203", "isbn"=>"1932-6203 (Electronic)\\r1932-6203 (Linking)", "doi"=>"10.1371/journal.pone.0029525", "pui"=>"363132796", "sgr"=>"84055207532", "pmid"=>"22216304", "scopus"=>"2-s2.0-84055207532"}, "id"=>"7334bce4-6eb8-3093-8f2f-f0c3e0727e49", "abstract"=>"Legionella pneumophila, which is the causative organism of Legionnaireś disease, translocates numerous effector proteins into the host cell cytosol by a type IV secretion system during infection. Among the most potent effector proteins of Legionella are glucosyltransferases (lgt's), which selectively modify eukaryotic elongation factor (eEF) 1A at Ser-53 in the GTP binding domain. Glucosylation results in inhibition of protein synthesis. Here we show that in vitro glucosylation of yeast and mouse eEF1A by Lgt3 in the presence of the factors Phe-tRNA(Phe) and GTP was enhanced 150 and 590-fold, respectively. The glucosylation of eEF1A catalyzed by Lgt1 and 2 was increased about 70-fold. By comparison of uncharged tRNA with two distinct aminoacyl-tRNAs (His-tRNA(His) and Phe-tRNA(Phe)) we could show that aminoacylation is crucial for Lgt-catalyzed glucosylation. Aminoacyl-tRNA had no effect on the enzymatic properties of lgt's and did not enhance the glucosylation rate of eEF1A truncation mutants, consisting of the GTPase domain only or of a 5 kDa peptide covering Ser-53 of eEF1A. Furthermore, binding of aminoacyl-tRNA to eEF1A was not altered by glucosylation. Taken together, our data suggest that the ternary complex, consisting of eEF1A, aminoacyl-tRNA and GTP, is the bona fide substrate for lgt's.", "link"=>"http://www.mendeley.com/research/aminoacyltrnacharged-eukaryotic-elongation-factor-1a-bona-fide-substrate-legionella-pneumophila-effe", "reader_count"=>13, "reader_count_by_academic_status"=>{"Professor > Associate Professor"=>1, "Researcher"=>3, "Student > Ph. D. Student"=>5, "Lecturer"=>1, "Professor"=>3}, "reader_count_by_user_role"=>{"Professor > Associate Professor"=>1, "Researcher"=>3, "Student > Ph. D. Student"=>5, "Lecturer"=>1, "Professor"=>3}, "reader_count_by_subject_area"=>{"Unspecified"=>1, "Biochemistry, Genetics and Molecular Biology"=>3, "Agricultural and Biological Sciences"=>6, "Medicine and Dentistry"=>1, "Chemistry"=>1, "Immunology and Microbiology"=>1}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>1}, "Chemistry"=>{"Chemistry"=>1}, "Immunology and Microbiology"=>{"Immunology and Microbiology"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>6}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>3}, "Unspecified"=>{"Unspecified"=>1}}, "reader_count_by_country"=>{"United States"=>1}, "group_count"=>0}

Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/700004"], "description"=>"<p>Wild type yeast eEF1A (yEF1A) and the yeast eEF1A S53A mutant (yEF1A S53A; each 1 µM) were subjected to an <i>in vitro</i> glucosylation reaction with Lgt3 (140 nM) in the presence or absence of Phe-tRNA<sup>Phe</sup>.</p>", "links"=>[], "tags"=>["eef1a", "glucosylation"], "article_id"=>370381, "categories"=>["Molecular Biology", "Biochemistry", "Microbiology", "Infectious Diseases"], "users"=>["Tina Tzivelekidis", "Thomas Jank", "Corinna Pohl", "Andreas Schlosser", "Sabine Rospert", "Charlotte R. Knudsen", "Marina V. Rodnina", "Yury Belyi", "Klaus Aktories"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0029525.g006", "stats"=>{"downloads"=>0, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Ser_53_in_eEF1A_is_the_unique_glucosylation_site_in_the_presence_of_Phe_tRNA_Phe_/370381", "title"=>"Ser-53 in eEF1A is the unique glucosylation site in the presence of Phe-tRNA<sup>Phe</sup>.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-12-22 00:06:21"}
  • {"files"=>["https://ndownloader.figshare.com/files/355654"], "description"=>"<div><p><em>Legionella pneumophila,</em> which is the causative organism of Legionnaireś disease, translocates numerous effector proteins into the host cell cytosol by a type IV secretion system during infection. Among the most potent effector proteins of <em>Legionella</em> are glucosyltransferases (lgt's), which selectively modify eukaryotic elongation factor (eEF) 1A at Ser-53 in the GTP binding domain. Glucosylation results in inhibition of protein synthesis. Here we show that <em>in vitro</em> glucosylation of yeast and mouse eEF1A by Lgt3 in the presence of the factors Phe-tRNA<sup>Phe</sup> and GTP was enhanced 150 and 590-fold, respectively. The glucosylation of eEF1A catalyzed by Lgt1 and 2 was increased about 70-fold. By comparison of uncharged tRNA with two distinct aminoacyl-tRNAs (His-tRNA<sup>His</sup> and Phe-tRNA<sup>Phe</sup>) we could show that aminoacylation is crucial for Lgt-catalyzed glucosylation. Aminoacyl-tRNA had no effect on the enzymatic properties of lgt's and did not enhance the glucosylation rate of eEF1A truncation mutants, consisting of the GTPase domain only or of a 5 kDa peptide covering Ser-53 of eEF1A. Furthermore, binding of aminoacyl-tRNA to eEF1A was not altered by glucosylation. Taken together, our data suggest that the ternary complex, consisting of eEF1A, aminoacyl-tRNA and GTP, is the <em>bona fide</em> substrate for lgt's.</p> </div>", "links"=>[], "tags"=>["aminoacyl-trna-charged", "eukaryotic", "elongation", "1a", "substrate", "effector", "glucosyltransferases"], "article_id"=>130275, "categories"=>["Molecular Biology", "Cancer", "Biochemistry", "Microbiology"], "users"=>["Tina Tzivelekidis", "Thomas Jank", "Corinna Pohl", "Andreas Schlosser", "Sabine Rospert", "Charlotte R. Knudsen", "Marina V. Rodnina", "Yury Belyi", "Klaus Aktories"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0029525", "stats"=>{"downloads"=>2, "page_views"=>13, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Aminoacyl_tRNA_Charged_Eukaryotic_Elongation_Factor_1A_Is_the_Bona_Fide_Substrate_for_Legionella_pneumophila_Effector_Glucosyltransferases/130275", "title"=>"Aminoacyl-tRNA-Charged Eukaryotic Elongation Factor 1A Is the <em>Bona Fide</em> Substrate for <em>Legionella pneumophila</em> Effector Glucosyltransferases", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2011-12-22 00:04:35"}
  • {"files"=>["https://ndownloader.figshare.com/files/699121"], "description"=>"<p>Mammalian eEF1A was isolated by eEF1Bα-affinity chromatography from RAW 264.7 macrophages infected with <i>L. pneumophila</i> wild type (A), <i>L. pneumophila</i> triple Δ<i>lgt</i>-mutant AM101 (B) and uninfected cells (C). LC-MS/MS (Q-TOF) analysis revealed the extracted ion chromatograms shown. The peak at m/z = 642.3 (2+) belongs to the chymotryptic peptide 43-EKEFAAEMGKGSF-54 of eEF1A without modification. This was identified by MS/MS with a Mascot peptide Score of 72. The peptide from <i>Legionella</i> infected cells is partially shifted to m/z = 723.3 (2+) indicating modification by hexose (162.053 Da). The chromatograms were scanned for peptides with m/z = 642.302±10 ppm (2+) (shown in blue) and peptides with m/z = 723.331±10 ppm (2+) (shown in red). The hexose-modified form of the peptide EKEFAAEMGKGSF was exclusively detected in <i>Legionella</i> infected cells. Partial neutral loss of dehydrohexose (162.053 Da), typical for hexose-modified peptides, is observed already without additional collision energy in the MS scan (see <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0029525#pone-0029525-g001\" target=\"_blank\">Figure 1A</a>, blue peak at 14 minutes). (D) Collision-induced dissociation MS/MS spectrum of the glucosylated peptide EKEFAAEMGKGSF (precursor m/z = 723.3 (2+); peak intensity = 2.5×10<sup>4</sup>; retention time 14.06 min) identified Ser-53 as the acceptor amino acid for glucosylation (Mascot peptide Score of 60).</p>", "links"=>[], "tags"=>["glucosylated"], "article_id"=>369511, "categories"=>["Molecular Biology", "Biochemistry", "Microbiology", "Infectious Diseases"], "users"=>["Tina Tzivelekidis", "Thomas Jank", "Corinna Pohl", "Andreas Schlosser", "Sabine Rospert", "Charlotte R. Knudsen", "Marina V. Rodnina", "Yury Belyi", "Klaus Aktories"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0029525.g001", "stats"=>{"downloads"=>0, "page_views"=>9, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_eEF1A_is_glucosylated_during_L_pneumophila_infection_at_Ser53_/369511", "title"=>"eEF1A is glucosylated during <i>L. pneumophila</i> infection at Ser53.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-12-22 02:38:31"}
  • {"files"=>["https://ndownloader.figshare.com/files/699448"], "description"=>"<p>(A) Time courses of the glucosylation of yeast eEF1A (yEF1A) with Lgt3 were performed in the presence of yeast tRNA (10 µM) and 10 µM UDP-[<sup>14</sup>C]glucose (triangles). Phe-tRNA synthetase was added at time point zero (black circles) or after 6 min (open circles) as marked by corresponding arrows. <sup>14</sup>C-glucosylation of yEF1A was determined by SDS-PAGE and autoradiography. Shown curves represent means (±SD) of three independent experiments. (B) Glucosylation of yEF1A (3 µM) by Lgt3 (5 nM) was conducted with increasing concentrations of HPLC-purified [<sup>14</sup>C]Phe-tRNA<sup>Phe</sup>. Initial glucosylation rates were determined after incubation for 10 min at 30°C in the presence of 50 µM GTPγS, 10 mM PEP, 0.1 mg/ml pyruvate kinase and 10 µM UDP-[<sup>14</sup>C]glucose as the donor substrate. Radiolabeled aa-tRNA could be distinguished from <sup>14</sup>C-glucosylated yEF1A by separation of the products by SDS-PAGE. Data shown represent velocities of yEF1A glucosylation and are given as means (±SD) of three independent experiments.</p>", "links"=>[], "tags"=>["stimulates", "eef1a"], "article_id"=>369827, "categories"=>["Molecular Biology", "Biochemistry", "Microbiology", "Infectious Diseases"], "users"=>["Tina Tzivelekidis", "Thomas Jank", "Corinna Pohl", "Andreas Schlosser", "Sabine Rospert", "Charlotte R. Knudsen", "Marina V. Rodnina", "Yury Belyi", "Klaus Aktories"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0029525.g003", "stats"=>{"downloads"=>0, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Aa_tRNA_stimulates_eEF1A_glucosylation_/369827", "title"=>"Aa-tRNA stimulates eEF1A glucosylation.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-12-22 02:43:47"}
  • {"files"=>["https://ndownloader.figshare.com/files/700100"], "description"=>"<p>Aminoacyl-tRNA stability towards hydrolysis was determined with 3 µM yeast eEF1A (yEF1A, filled circles) or glucosylated yeast eEF1A (yEF1A, open circles), 1 mM GTP and 1 µM [<sup>14</sup>C]Phe-tRNA<sup>Phe</sup> for 60 min. As a control [<sup>14</sup>C]Phe-tRNA<sup>Phe</sup> was incubated without eEF1A (triangles). Non-hydrolyzed [<sup>14</sup>C]Phe-tRNA<sup>Phe</sup> was quantified by filter binding assay and scintillation counting.</p>", "links"=>[], "tags"=>["glucosylation", "ternary"], "article_id"=>370479, "categories"=>["Molecular Biology", "Biochemistry", "Microbiology", "Infectious Diseases"], "users"=>["Tina Tzivelekidis", "Thomas Jank", "Corinna Pohl", "Andreas Schlosser", "Sabine Rospert", "Charlotte R. Knudsen", "Marina V. Rodnina", "Yury Belyi", "Klaus Aktories"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0029525.g007", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Effect_of_glucosylation_on_the_stability_of_the_ternary_complex_/370479", "title"=>"Effect of glucosylation on the stability of the ternary complex.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-12-22 00:07:59"}
  • {"files"=>["https://ndownloader.figshare.com/files/699627"], "description"=>"<p>Time courses of glucosylation of purified yeast eEF1A (yEF1A) (A) or mouse eEF1A (mEF1A) (B) by Lgt3 in the absence (triangles) or presence of Phe-tRNA<sup>Phe</sup> (filled circles) or uncharged tRNA<sup>Phe</sup> (open circles). The glucosylation reactions and analyses were performed under the conditions as described in <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0029525#pone-0029525-g001\" target=\"_blank\">Figure 1</a>. Values of <sup>14</sup>C-glucose incorporation are shown as the mean (±SD) of at least three independent experiments. The inserts show representative radioimages. (C) eEF1A ternary complex is quantitatively glucosylated by Lgt3. Yeast eEF1A (20 µM) was glucosylated by Lgt3 (5 µM) with Phe-tRNA<sup>Phe</sup> (20 µM) and GTP (75 µM) in the absence (lane 1) or presence (lane 2) of cold UDP-glucose (1 mM). Modified and unmodified yEF1A were separated by His-eEF1Bα affinity purification as described in <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0029525#s4\" target=\"_blank\">Materials and Methods</a>. Thereafter, the isolated eEF1A (3 µM each) was subjected to second glucosylation reaction with radiolabeled UDP-[<sup>14</sup>C]glucose in presence of Phe-tRNA<sup>Phe</sup> (1 µM) and GTP (75 µM). The Coomassie gel and the autoradiogram are shown. (D) Glucosylation of yEF1A (2 µM) was performed in the presence of His-tRNA<sup>His</sup> or uncharged yeast tRNA with Lgt3 (140 nM).</p>", "links"=>[], "tags"=>["eef1a", "glucosylation"], "article_id"=>369998, "categories"=>["Molecular Biology", "Biochemistry", "Microbiology", "Infectious Diseases"], "users"=>["Tina Tzivelekidis", "Thomas Jank", "Corinna Pohl", "Andreas Schlosser", "Sabine Rospert", "Charlotte R. Knudsen", "Marina V. Rodnina", "Yury Belyi", "Klaus Aktories"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0029525.g004", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Kinetics_of_eEF1A_glucosylation_by_Lgt3_/369998", "title"=>"Kinetics of eEF1A glucosylation by Lgt3.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-12-22 02:46:38"}
  • {"files"=>["https://ndownloader.figshare.com/files/700257"], "description"=>"<p>Yeast eEF1A (yEF1A) and mouse eEF1A (mEF1A) were incubated for 10 min with an equimolar concentration of HPLC-purified Phe-tRNA<sup>Phe</sup> and GTPγS or GDPβS (50 µM) as indicated. Afterwards the complexes were subjected to <i>in vitro</i> glucosyltransferase reactions with UDP-[<sup>14</sup>C]glucose (10 µM) and 5 nM Lgt1, 2 and 3. The data were autoradiographically quantified using ImageQuant. Data are given as the mean (±SD) of triplicates of 5 min time points.</p>", "links"=>[], "tags"=>["glucosylation", "eef1a", "ternary"], "article_id"=>370634, "categories"=>["Molecular Biology", "Biochemistry", "Microbiology", "Infectious Diseases"], "users"=>["Tina Tzivelekidis", "Thomas Jank", "Corinna Pohl", "Andreas Schlosser", "Sabine Rospert", "Charlotte R. Knudsen", "Marina V. Rodnina", "Yury Belyi", "Klaus Aktories"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0029525.t001", "stats"=>{"downloads"=>4, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_k_cat_values_for_glucosylation_of_eEF1A_ternary_complex_by_Lgt_s_/370634", "title"=>"<i>k</i><sub>cat</sub>-values for glucosylation of eEF1A ternary complex by Lgt's.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2011-12-22 00:10:34"}
  • {"files"=>["https://ndownloader.figshare.com/files/699822"], "description"=>"<p>(A) Schematic representation of the eEF1A truncations used (upper panel). Lower panel: Structural models deduced from the crystal structure of eEF1A in complex with eEF1B (pdb 1IJF). For visualization of the region of aminoacyl-tRNA binding the crystal structure of the ternary complex of EF-Tu•GTP•Phe-tRNA<sup>Phe</sup> (pdb 1TTT) is depicted on the right. The GTPase domain (G domain) is shaded in orange, domain II in blue, domain III in green, and tRNA is shown in brown. The aminoacyl residue of aa-tRNA located between the G domain and domain II is shown as red spheres. GDP or GTP is depicted as black sticks. The position of glucosyl acceptor serine 53 is shown in red and marked with arrowheads. The figures were prepared using PyMOL (<a href=\"http://www.pymol.org\" target=\"_blank\">www.pymol.org</a>). (B) Glucosylation of different truncation fragments of yeast eEF1A (yEF1A) (3 µM) was performed with Lgt3 (140 nM) in the presence of Phe-tRNA<sup>Phe</sup> or uncharged tRNA<sup>Phe</sup> (each 1 µM), respectively. Constructs used: p38 represent eEF1A without domain III (aa1-349), p29 harbors the G domain (aa1-265), and p5 is a 5 kDa-peptide, comprising the helix-loop-helix region (aa29-73) of yEF1A. Glucosylation was performed under standard conditions for 15 min at 30°C. The insert shows the induction of Lgt3-catalyzed glucosylation of the fragments by Phe-tRNA<sup>Phe</sup>. (C) Time courses of <i>in vitro</i> glucosylation of yEF1A in complex with GTP and Phe-tRNA<sup>Phe</sup> (open circles), the 45 amino acid fragment of yEF1A p5 (filled squares), yEF1A (filled circles), and yEF1A with uncharged tRNA<sup>Phe</sup> (open triangles) by Lgt3. All data given represent means (±SD) of three independent experiments.</p>", "links"=>[], "tags"=>["eef1a", "constructs", "glucosylation"], "article_id"=>370199, "categories"=>["Molecular Biology", "Biochemistry", "Microbiology", "Infectious Diseases"], "users"=>["Tina Tzivelekidis", "Thomas Jank", "Corinna Pohl", "Andreas Schlosser", "Sabine Rospert", "Charlotte R. Knudsen", "Marina V. Rodnina", "Yury Belyi", "Klaus Aktories"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0029525.g005", "stats"=>{"downloads"=>1, "page_views"=>11, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Models_of_eEF1A_constructs_and_activity_of_Lgt_s_in_glucosylation_of_eEF1A_fragments_/370199", "title"=>"Models of eEF1A constructs and activity of Lgt's in glucosylation of eEF1A fragments.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-12-22 00:03:19"}
  • {"files"=>["https://ndownloader.figshare.com/files/699249"], "description"=>"<p>(A) Glucosyltransferase reaction was performed with Lgt3 (140 nM) and yeast eEF1A (3 µM) with UDP-[<sup>14</sup>C]glucose (10 µM) for 15 min at 30°C in the presence of either GDPβS (75 µM) or GTPγS (75 µM) and the following components: purified yeast eEF1A (control, lane 1), yEF1A with freshly prepared yeast cell lysate (30 µg) (lane 2 and 3), yEF1A in the presence of GDPβS (75 µM) (lane 4) or GTPγS (75 µM) (lane 5), yEF1A·yEF1Bα complex (3 µM each) (lane 6), yEF1A with 5 µl phenol/chloroform extract (P/C extract) prepared from yeast lysate (lane 7 and 8). Prior to glucosyltransferase reaction, the mixtures were preincubated for 10 min at RT. Products were separated by SDS-PAGE and glucosylated eEF1A was visualized by autoradiography. (B) Effect of the RNase A treatment. Glucosylation of 3 µM eEF1A by Lgt3 (140 nM) in yeast lysate or with P/C-extract was performed after treatment with RNase A (1.6 mg/ml) for 10 min at RT. (C) Glucosyltransferase reaction was performed as in (A) with the addition of Phe-tRNA<sup>Phe</sup> or uncharged yeast tRNA<sup>Phe</sup> (1 µM) in the presence of GDPβS (75 µM) or GTPγS (75 µM), respectively.</p>", "links"=>[], "tags"=>["yeast", "eef1a", "glucosylation"], "article_id"=>369633, "categories"=>["Molecular Biology", "Biochemistry", "Microbiology", "Infectious Diseases"], "users"=>["Tina Tzivelekidis", "Thomas Jank", "Corinna Pohl", "Andreas Schlosser", "Sabine Rospert", "Charlotte R. Knudsen", "Marina V. Rodnina", "Yury Belyi", "Klaus Aktories"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0029525.g002", "stats"=>{"downloads"=>0, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Analysis_of_yeast_eEF1A_yEF1A_glucosylation_by_Lgt3_/369633", "title"=>"Analysis of yeast eEF1A (yEF1A) glucosylation by Lgt3.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-12-22 02:40:33"}

PMC Usage Stats | Further Information

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