The Cell Wall-Associated Mycolactone Polyketide Synthases Are Necessary but Not Sufficient for Mycolactone Biosynthesis
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{"title"=>"The Cell Wall-Associated Mycolactone Polyketide Synthases Are Necessary but Not Sufficient for Mycolactone Biosynthesis", "type"=>"journal", "authors"=>[{"first_name"=>"Jessica L.", "last_name"=>"Porter", "scopus_author_id"=>"8593697900"}, {"first_name"=>"Nicholas J.", "last_name"=>"Tobias", "scopus_author_id"=>"27968115300"}, {"first_name"=>"Sacha J.", "last_name"=>"Pidot", "scopus_author_id"=>"15842042600"}, {"first_name"=>"Steffen", "last_name"=>"Falgner", "scopus_author_id"=>"57199516577"}, {"first_name"=>"Kellie L.", "last_name"=>"Tuck", "scopus_author_id"=>"55880466600"}, {"first_name"=>"Andrea", "last_name"=>"Vettiger", "scopus_author_id"=>"55363006400"}, {"first_name"=>"Hui", "last_name"=>"Hong", "scopus_author_id"=>"55722856800"}, {"first_name"=>"Peter F.", "last_name"=>"Leadlay", "scopus_author_id"=>"7006856285"}, {"first_name"=>"Timothy P.", "last_name"=>"Stinear", "scopus_author_id"=>"6602594923"}], "year"=>2013, "source"=>"PLoS ONE", "identifiers"=>{"issn"=>"19326203", "scopus"=>"2-s2.0-84880708925", "pui"=>"369423969", "doi"=>"10.1371/journal.pone.0070520", "isbn"=>"1932-6203 (Electronic)\\r1932-6203 (Linking)", "sgr"=>"84880708925", "pmid"=>"23894666"}, "id"=>"00d3e83e-f3b3-3139-a37b-de04a73975c1", "abstract"=>"Mycolactones are polyketide-derived lipid virulence factors made by the slow-growing human pathogen, Mycobacterium ulcerans. Three unusually large and homologous plasmid-borne genes (mlsA1: 51 kb, mlsB: 42 kb and mlsA2: 7 kb) encode the mycolactone type I polyketide synthases (PKS). The extreme size and low sequence diversity of these genes has posed significant barriers for exploration of the genetic and biochemical basis of mycolactone synthesis. Here, we have developed a truncated, more tractable 3-module version of the 18-module mycolactone PKS and we show that this engineered PKS functions as expected in the natural host M. ulcerans to produce an additional polyketide; a triketide lactone (TKL). Cell fractionation experiments indicated that this 3-module PKS and the putative accessory enzymes encoded by mup045 and mup038 associated with the mycobacterial cell wall, a finding supported by confocal microscopy. We then assessed the capacity of the faster growing, Mycobacterium marinum to harbor and express the 3-module Mls PKS and accessory enzymes encoded by mup045 and mup038. RT-PCR, immunoblotting, and cell fractionation experiments confirmed that the truncated Mls PKS multienzymes were expressed and also partitioned with the cell wall material in M. marinum. However, this heterologous host failed to produce TKL. The systematic deconstruction of the mycolactone PKS presented here suggests that the Mls multienzymes are necessary but not sufficient for mycolactone synthesis and that synthesis is likely to occur (at least in part) within the mycobacterial cell wall. This research is also the first proof-of-principle demonstration of the potential of this enzyme complex to produce tailored small molecules through genetically engineered rearrangements of the Mls modules.", "link"=>"http://www.mendeley.com/research/cell-wallassociated-mycolactone-polyketide-synthases-necessary-not-sufficient-mycolactone-biosynthes", "reader_count"=>20, "reader_count_by_academic_status"=>{"Professor > Associate Professor"=>1, "Student > Doctoral Student"=>4, "Researcher"=>4, "Student > Ph. D. Student"=>3, "Student > Master"=>6, "Other"=>1, "Student > Bachelor"=>1}, "reader_count_by_user_role"=>{"Professor > Associate Professor"=>1, "Student > Doctoral Student"=>4, "Researcher"=>4, "Student > Ph. D. Student"=>3, "Student > Master"=>6, "Other"=>1, "Student > Bachelor"=>1}, "reader_count_by_subject_area"=>{"Biochemistry, Genetics and Molecular Biology"=>2, "Agricultural and Biological Sciences"=>13, "Medicine and Dentistry"=>1, "Chemistry"=>2, "Psychology"=>1, "Immunology and Microbiology"=>1}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>1}, "Chemistry"=>{"Chemistry"=>2}, "Psychology"=>{"Psychology"=>1}, "Immunology and Microbiology"=>{"Immunology and Microbiology"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>13}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>2}}, "group_count"=>0}

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/1127583"], "description"=>"<p>Depicted also is the proposed biosynthetic process for synthesis of the lactone core and upper side chain of mycolactone. Shown in inset (left) is the domain structure of the <i>mlsB</i> loading module from <i>M. ulcerans</i> Liflandii, showing the AT-propionate domain with propionate starter unit <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0070520#pone.0070520-Pidot1\" target=\"_blank\">[13]</a>.</p>", "links"=>[], "tags"=>["Biochemistry", "chemical biology", "lipids", "biotechnology", "Applied microbiology", "microbiology", "bacteriology", "Bacterial biochemistry", "Medical microbiology", "Infectious diseases", "Bacterial diseases", "Nontuberculous mycobacteria", "module", "mlsa1", "mlsa2", "mycolactone", "harboured", "plasmid", "pmum001", "agy99"], "article_id"=>752429, "categories"=>["Biological Sciences", "Medicine"], "users"=>["Jessica L. Porter", "Nicholas J. Tobias", "Sacha J. Pidot", "Steffen Falgner", "Kellie L. Tuck", "Andrea Vettiger", "Hui Hong", "Peter F. Leadlay", "Timothy P. Stinear"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0070520.g001", "stats"=>{"downloads"=>9, "page_views"=>187, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Overview_of_gene_module_and_domain_organization_of_MlsA1_and_MlsA2_from_the_mycolactone_PKS_harboured_by_the_plasmid_pMUM001_from_i_M_ulcerans_i_Agy99_10_/752429", "title"=>"Overview of gene, module and domain organization of MlsA1 and MlsA2 from the mycolactone PKS, harboured by the plasmid pMUM001 from <i>M. ulcerans</i> Agy99 [10].", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-07-23 08:04:14"}
  • {"files"=>["https://ndownloader.figshare.com/files/1127600"], "description"=>"<div><p>Mycolactones are polyketide-derived lipid virulence factors made by the slow-growing human pathogen, <i>Mycobacterium ulcerans</i>. Three unusually large and homologous plasmid-borne genes (<i>mlsA1</i>: 51 kb, <i>mlsB</i>: 42 kb and <i>mlsA2</i>: 7 kb) encode the mycolactone type I polyketide synthases (PKS). The extreme size and low sequence diversity of these genes has posed significant barriers for exploration of the genetic and biochemical basis of mycolactone synthesis. Here, we have developed a truncated, more tractable 3-module version of the 18-module mycolactone PKS and we show that this engineered PKS functions as expected in the natural host <i>M. ulcerans</i> to produce an additional polyketide; a triketide lactone (TKL). Cell fractionation experiments indicated that this 3-module PKS and the putative accessory enzymes encoded by mup045 and mup038 associated with the mycobacterial cell wall, a finding supported by confocal microscopy. We then assessed the capacity of the faster growing, <i>Mycobacterium marinum</i> to harbor and express the 3-module Mls PKS and accessory enzymes encoded by mup045 and mup038. RT-PCR, immunoblotting, and cell fractionation experiments confirmed that the truncated Mls PKS multienzymes were expressed and also partitioned with the cell wall material in <i>M. marinum.</i> However, this heterologous host failed to produce TKL. The systematic deconstruction of the mycolactone PKS presented here suggests that the Mls multienzymes are necessary but not sufficient for mycolactone synthesis and that synthesis is likely to occur (at least in part) within the mycobacterial cell wall. This research is also the first proof-of-principle demonstration of the potential of this enzyme complex to produce tailored small molecules through genetically engineered rearrangements of the Mls modules.</p></div>", "links"=>[], "tags"=>["Biochemistry", "chemical biology", "lipids", "biotechnology", "Applied microbiology", "microbiology", "bacteriology", "Bacterial biochemistry", "Medical microbiology", "Infectious diseases", "Bacterial diseases", "Nontuberculous mycobacteria", "wall-associated", "mycolactone", "polyketide", "synthases"], "article_id"=>752446, "categories"=>["Biological Sciences", "Medicine"], "users"=>["Jessica L. Porter", "Nicholas J. Tobias", "Sacha J. Pidot", "Steffen Falgner", "Kellie L. Tuck", "Andrea Vettiger", "Hui Hong", "Peter F. Leadlay", "Timothy P. Stinear"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0070520", "stats"=>{"downloads"=>2, "page_views"=>14, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/The_Cell_Wall_Associated_Mycolactone_Polyketide_Synthases_Are_Necessary_but_Not_Sufficient_for_Mycolactone_Biosynthesis/752446", "title"=>"The Cell Wall-Associated Mycolactone Polyketide Synthases Are Necessary but Not Sufficient for Mycolactone Biosynthesis", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-07-23 08:04:14"}
  • {"files"=>["https://ndownloader.figshare.com/files/1127597"], "description"=>"<p>Cells were stained with DAPI and incubated with a primary anti-Mup045 antibody with visualization by a secondary antibody conjugated to Alexa fluor-568.</p>", "links"=>[], "tags"=>["Biochemistry", "chemical biology", "lipids", "biotechnology", "Applied microbiology", "microbiology", "bacteriology", "Bacterial biochemistry", "Medical microbiology", "Infectious diseases", "Bacterial diseases", "Nontuberculous mycobacteria", "mup045", "mycobacterial", "06-3844", "compared", "revealed", "dic", "fluorescence"], "article_id"=>752443, "categories"=>["Biological Sciences", "Medicine"], "users"=>["Jessica L. Porter", "Nicholas J. Tobias", "Sacha J. Pidot", "Steffen Falgner", "Kellie L. Tuck", "Andrea Vettiger", "Hui Hong", "Peter F. Leadlay", "Timothy P. Stinear"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0070520.g010", "stats"=>{"downloads"=>0, "page_views"=>34, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Imaging_of_Mup045_in_association_with_the_mycobacterial_cell_wall_in_i_M_ulcerans_i_06_3844_wild_type_compared_with_i_M_marinum_i_M_wild_type_as_revealed_by_DIC_fluorescence_microscopy_/752443", "title"=>"Imaging of Mup045 in association with the mycobacterial cell wall in <i>M. ulcerans</i> 06-3844 wild type compared with <i>M. marinum</i> M wild type, as revealed by DIC fluorescence microscopy.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-07-23 08:04:14"}
  • {"files"=>["https://ndownloader.figshare.com/files/1127590"], "description"=>"<p>A late log-phase culture of <i>M. marinum</i> harbouring pTPS629 (and <i>mlsA2</i> on pTPS334) grown in the presence of apramycin and hygromycin, was shifted to media without apramycin and then monitored at successive time points by determining the cfu/ml on media with the antibiotic (squares) and calculating the percentage of <i>M. marinum</i> cells retaining apramycin resistance (right hand Y-axis, triangles). These results depict the mean and standard deviation of at least biological triplicates.</p>", "links"=>[], "tags"=>["Biochemistry", "chemical biology", "lipids", "biotechnology", "Applied microbiology", "microbiology", "bacteriology", "Bacterial biochemistry", "Medical microbiology", "Infectious diseases", "Bacterial diseases", "Nontuberculous mycobacteria", "ptps629", "cultured", "apramycin", "antibiotic"], "article_id"=>752436, "categories"=>["Biological Sciences", "Medicine"], "users"=>["Jessica L. Porter", "Nicholas J. Tobias", "Sacha J. Pidot", "Steffen Falgner", "Kellie L. Tuck", "Andrea Vettiger", "Hui Hong", "Peter F. Leadlay", "Timothy P. Stinear"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0070520.g006", "stats"=>{"downloads"=>0, "page_views"=>8, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Stability_of_pTPS629_in_i_M_marinum_i_M_cultured_in_the_absence_of_apramycin_antibiotic_selection_/752436", "title"=>"Stability of pTPS629 in <i>M. marinum</i> M cultured in the absence of apramycin antibiotic selection.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-07-23 08:04:14"}
  • {"files"=>["https://ndownloader.figshare.com/files/1127587"], "description"=>"<p>(A) SDS-PAGE separation and Coomassie-stained protein of 10 μg of <i>M. ulcerans</i> 06-3844 containing <i>mlsA1</i> LM-M8 (TPS8162), LM<sub>P</sub>-M8 (TPS8307) or empty vector (TPS8164) cell fractions (B) Western immunoblot analysis of (A) with an anti-AT domain antibody showing the presence of a ∼400 kDa protein produced by <i>M. ulcerans</i> harbouring either LM-M8 or LM<sub>P</sub>-M8 (lane 1 and 4). Positive control is purified, recombinant acyltransferase derived from MlsA2.</p>", "links"=>[], "tags"=>["Biochemistry", "chemical biology", "lipids", "biotechnology", "Applied microbiology", "microbiology", "bacteriology", "Bacterial biochemistry", "Medical microbiology", "Infectious diseases", "Bacterial diseases", "Nontuberculous mycobacteria", "immunoblot", "06-3844", "expressing", "tkl"], "article_id"=>752433, "categories"=>["Biological Sciences", "Medicine"], "users"=>["Jessica L. Porter", "Nicholas J. Tobias", "Sacha J. Pidot", "Steffen Falgner", "Kellie L. Tuck", "Andrea Vettiger", "Hui Hong", "Peter F. Leadlay", "Timothy P. Stinear"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0070520.g004", "stats"=>{"downloads"=>0, "page_views"=>13, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/SDS_PAGE_and_western_immunoblot_analysis_of_i_M_ulcerans_i_06_3844_expressing_TKL_constructs_/752433", "title"=>"SDS-PAGE and western immunoblot analysis of <i>M. ulcerans</i> 06-3844 expressing TKL constructs.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-07-23 08:04:14"}
  • {"files"=>["https://ndownloader.figshare.com/files/1127586"], "description"=>"<p>(A) Arrangement using the MlsA1 load module from <i>M. ulcerans</i> Agy99 for the biosynthesis of methyl-triketide lactone; (B) Arrangement using the MlsA1 load module from <i>M. ulcerans</i> Liflandii for the biosynthesis of ethyl-triketide lactone.</p>", "links"=>[], "tags"=>["Biochemistry", "chemical biology", "lipids", "biotechnology", "Applied microbiology", "microbiology", "bacteriology", "Bacterial biochemistry", "Medical microbiology", "Infectious diseases", "Bacterial diseases", "Nontuberculous mycobacteria", "module", "organisation", "bimodular", "mlsa-derived"], "article_id"=>752432, "categories"=>["Biological Sciences", "Medicine"], "users"=>["Jessica L. Porter", "Nicholas J. Tobias", "Sacha J. Pidot", "Steffen Falgner", "Kellie L. Tuck", "Andrea Vettiger", "Hui Hong", "Peter F. Leadlay", "Timothy P. Stinear"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0070520.g003", "stats"=>{"downloads"=>0, "page_views"=>12, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Gene_module_and_domain_organisation_in_the_bimodular_MlsA_derived_PKS_/752432", "title"=>"Gene, module and domain organisation in the bimodular MlsA-derived PKS.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-07-23 08:04:14"}
  • {"files"=>["https://ndownloader.figshare.com/files/1127599"], "description"=>"*<p>LM-M8 refers to the loading module and module 8 regions encoded within <i>mlsA1</i>; LM<sub>P</sub>-M8 refers to the loading module from <i>M. ulcerans</i> Liflandii <i>mlsB</i> fused with <i>mlsA1</i> M8 from <i>M. ulcerans</i> Agy99.</p>", "links"=>[], "tags"=>["Biochemistry", "chemical biology", "lipids", "biotechnology", "Applied microbiology", "microbiology", "bacteriology", "Bacterial biochemistry", "Medical microbiology", "Infectious diseases", "Bacterial diseases", "Nontuberculous mycobacteria"], "article_id"=>752445, "categories"=>["Biological Sciences", "Medicine"], "users"=>["Jessica L. Porter", "Nicholas J. Tobias", "Sacha J. Pidot", "Steffen Falgner", "Kellie L. Tuck", "Andrea Vettiger", "Hui Hong", "Peter F. Leadlay", "Timothy P. Stinear"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0070520.t002", "stats"=>{"downloads"=>0, "page_views"=>2, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Plasmids_used_in_this_study_/752445", "title"=>"Plasmids used in this study.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-07-23 08:04:14"}
  • {"files"=>["https://ndownloader.figshare.com/files/1127584"], "description"=>"<p>(A) pTPS333, pYUB412-based integrating vector with <i>mlsA1</i> LM-M8 under the control of the <i>mlsA1</i> promoter; (B) pTPS629, pMUM001-based low-copy number vector with <i>mlsA1</i> LM-M8 under the control of the <i>mlsA1</i> promoter; (C) pTPS334, pYUB412-based integrating vector with <i>mlsA2</i> under the control of the <i>mlsA1</i> promoter; (D) pTPS338 pMV261-based vector with mup038 and mup045 in an operon and under the control of the <i>ermE</i> promoter.</p>", "links"=>[], "tags"=>["Biochemistry", "chemical biology", "lipids", "biotechnology", "Applied microbiology", "microbiology", "bacteriology", "Bacterial biochemistry", "Medical microbiology", "Infectious diseases", "Bacterial diseases", "Nontuberculous mycobacteria", "mycobacterial", "vectors", "developed"], "article_id"=>752430, "categories"=>["Biological Sciences", "Medicine"], "users"=>["Jessica L. Porter", "Nicholas J. Tobias", "Sacha J. Pidot", "Steffen Falgner", "Kellie L. Tuck", "Andrea Vettiger", "Hui Hong", "Peter F. Leadlay", "Timothy P. Stinear"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0070520.g002", "stats"=>{"downloads"=>1, "page_views"=>22, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Schematic_view_of_the_mycobacterial_expression_vectors_developed_for_this_study_/752430", "title"=>"Schematic view of the mycobacterial expression vectors developed for this study.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-07-23 08:04:14"}
  • {"files"=>["https://ndownloader.figshare.com/files/1127598"], "description"=>"<p>Bacterial strains used in the study.</p>", "links"=>[], "tags"=>["Biochemistry", "chemical biology", "lipids", "biotechnology", "Applied microbiology", "microbiology", "bacteriology", "Bacterial biochemistry", "Medical microbiology", "Infectious diseases", "Bacterial diseases", "Nontuberculous mycobacteria", "strains"], "article_id"=>752444, "categories"=>["Biological Sciences", "Medicine"], "users"=>["Jessica L. Porter", "Nicholas J. Tobias", "Sacha J. Pidot", "Steffen Falgner", "Kellie L. Tuck", "Andrea Vettiger", "Hui Hong", "Peter F. Leadlay", "Timothy P. Stinear"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0070520.t001", "stats"=>{"downloads"=>0, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Bacterial_strains_used_in_the_study_/752444", "title"=>"Bacterial strains used in the study.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-07-23 08:04:14"}
  • {"files"=>["https://ndownloader.figshare.com/files/1127595"], "description"=>"<p>(A) Coomassie stained SDS-PAGE and (B) Western immunoblot of cell wall fractions of <i>M. marinum</i> expressing LM-M8, MlsA2<sub>His</sub>, Mup038 and Mup045 (TPS8334) using an anti-AT domain antibody demonstrating the presence of the heterologously expressed PKSs in the cell wall fraction of this strain. The positive control is purified, recombinant acyltransferase from MlsA2.</p>", "links"=>[], "tags"=>["Biochemistry", "chemical biology", "lipids", "biotechnology", "Applied microbiology", "microbiology", "bacteriology", "Bacterial biochemistry", "Medical microbiology", "Infectious diseases", "Bacterial diseases", "Nontuberculous mycobacteria", "recombinant"], "article_id"=>752441, "categories"=>["Biological Sciences", "Medicine"], "users"=>["Jessica L. Porter", "Nicholas J. Tobias", "Sacha J. Pidot", "Steffen Falgner", "Kellie L. Tuck", "Andrea Vettiger", "Hui Hong", "Peter F. Leadlay", "Timothy P. Stinear"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0070520.g009", "stats"=>{"downloads"=>0, "page_views"=>17, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Expression_analysis_of_recombinant_i_M_marinum_i_TPS8334_/752441", "title"=>"Expression analysis of recombinant <i>M. marinum</i> TPS8334.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-07-23 08:04:14"}
  • {"files"=>["https://ndownloader.figshare.com/files/1127593"], "description"=>"<p>(A) RT-PCR of mup045, mup038 and <i>crtI</i> on RNA extracted from <i>M. marinum</i> M containing plasmids expressing LM-M8 and mup045-mup038 under control of the P<i><sub>ermE</sub></i> promoter. Western immunoblots showing: (B) presence of Mup038 in the cell wall fraction of <i>M. marinum</i> TPS8334; (C) presence of Mup045 in whole cell lysates from <i>M. marinum</i> M expressing LM-M8 and mup045-mup038 (TPS8334) as well as <i>M. ulcerans</i> 06-3844 harbouring pTPS331 (TPS8164) or pTPS333 (TPS8162); (D) Localization of Mup045 to the cell wall in <i>M. ulcerans</i> 06-3844 wild type and <i>M. marinum</i> TPS8334 cell fractions, showing reactivity against Mup045 in all strains, and localized to the cell wall fraction in both strains. Positive controls are purified, recombinant Mup038 and Mup045. (D).</p>", "links"=>[], "tags"=>["Biochemistry", "chemical biology", "lipids", "biotechnology", "Applied microbiology", "microbiology", "bacteriology", "Bacterial biochemistry", "Medical microbiology", "Infectious diseases", "Bacterial diseases", "Nontuberculous mycobacteria", "mycolactone", "accessory", "enzymes", "encoded", "mup045"], "article_id"=>752439, "categories"=>["Biological Sciences", "Medicine"], "users"=>["Jessica L. Porter", "Nicholas J. Tobias", "Sacha J. Pidot", "Steffen Falgner", "Kellie L. Tuck", "Andrea Vettiger", "Hui Hong", "Peter F. Leadlay", "Timothy P. Stinear"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0070520.g008", "stats"=>{"downloads"=>1, "page_views"=>11, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Expression_of_mycolactone_accessory_enzymes_encoded_by_mup045_and_mup038_/752439", "title"=>"Expression of mycolactone accessory enzymes encoded by mup045 and mup038.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-07-23 08:04:14"}
  • {"files"=>["https://ndownloader.figshare.com/files/1127592"], "description"=>"<p>(A) SDS-PAGE separation and Coomassie-stained protein gel of 10 μg of whole cell lysate of <i>M. marinum</i> M with LM-M8 and <i>mlsA2</i> (TPS8313) and empty vector control (TPS8256); (B) Western immunoblot of (A) using an anti-AT domain antibody; (C) Western immunoblot of (A) using an anti-His antibody; (D) Western immunoblot of cell fractions from <i>M. marinum</i> M harbouring plasmids expressing LM-M8 and MlsA2<sub>His</sub> using an anti-His antibody, showing MlsA2 is present only in the cell wall (P27) fraction. The reactivity of the anti-His antibody to a protein with a mass ∼65 kDa in panels (C) and (D) is the known cross-reactivity with the polyhistidines of mycobacterial GroEL (Hsp65) <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0070520#pone.0070520-Noens1\" target=\"_blank\">[37]</a>.</p>", "links"=>[], "tags"=>["Biochemistry", "chemical biology", "lipids", "biotechnology", "Applied microbiology", "microbiology", "bacteriology", "Bacterial biochemistry", "Medical microbiology", "Infectious diseases", "Bacterial diseases", "Nontuberculous mycobacteria", "immunoblot", "lysates", "fractions", "harbouring", "plasmids", "expressing", "lm-m8"], "article_id"=>752438, "categories"=>["Biological Sciences", "Medicine"], "users"=>["Jessica L. Porter", "Nicholas J. Tobias", "Sacha J. Pidot", "Steffen Falgner", "Kellie L. Tuck", "Andrea Vettiger", "Hui Hong", "Peter F. Leadlay", "Timothy P. Stinear"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0070520.g007", "stats"=>{"downloads"=>0, "page_views"=>32, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/SDS_PAGE_and_western_immunoblot_analysis_of_whole_cell_lysates_and_cell_fractions_of_i_M_marinum_i_M_harbouring_plasmids_expressing_LM_M8_and_MlsA2_sub_His_sub_/752438", "title"=>"SDS-PAGE and western immunoblot analysis of whole cell lysates and cell fractions of <i>M. marinum</i> M harbouring plasmids expressing LM-M8 and MlsA2<sub>His</sub>.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-07-23 08:04:14"}
  • {"files"=>["https://ndownloader.figshare.com/files/1127589"], "description"=>"<p>(A) control; (B) sample and (C) standard compound, 5-Hydroxyhexanoic acid lactone. Insets are the MS/MS spectrum for [M+H]+ ion at m/z 115.</p>", "links"=>[], "tags"=>["Biochemistry", "chemical biology", "lipids", "biotechnology", "Applied microbiology", "microbiology", "bacteriology", "Bacterial biochemistry", "Medical microbiology", "Infectious diseases", "Bacterial diseases", "Nontuberculous mycobacteria", "ions", "ion"], "article_id"=>752435, "categories"=>["Biological Sciences", "Medicine"], "users"=>["Jessica L. Porter", "Nicholas J. Tobias", "Sacha J. Pidot", "Steffen Falgner", "Kellie L. Tuck", "Andrea Vettiger", "Hui Hong", "Peter F. Leadlay", "Timothy P. Stinear"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0070520.g005", "stats"=>{"downloads"=>0, "page_views"=>7, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Chromatogram_of_fragment_ions_at_m_z_73_3_and_97_3_from_MS_MS_analysis_of_M_H_ion_at_m_z_115_1_/752435", "title"=>"Chromatogram of fragment ions at m/z 73.3 and 97.3 from MS/MS analysis of [M+H]+ ion at m/z 115.1.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-07-23 08:04:14"}

PMC Usage Stats | Further Information

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Relative Metric

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