An Efficient Strategy for Small-Scale Screening and Production of Archaeal Membrane Transport Proteins in Escherichia coli
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{"title"=>"An Efficient Strategy for Small-Scale Screening and Production of Archaeal Membrane Transport Proteins in Escherichia coli", "type"=>"journal", "authors"=>[{"first_name"=>"Pikyee", "last_name"=>"Ma", "scopus_author_id"=>"17135308700"}, {"first_name"=>"Filipa", "last_name"=>"Varela", "scopus_author_id"=>"55839483300"}, {"first_name"=>"Malgorzata", "last_name"=>"Magoch", "scopus_author_id"=>"55265642600"}, {"first_name"=>"Ana Rita", "last_name"=>"Silva", "scopus_author_id"=>"55900987800"}, {"first_name"=>"Ana Lúcia", "last_name"=>"Rosário", "scopus_author_id"=>"36244135300"}, {"first_name"=>"José", "last_name"=>"Brito", "scopus_author_id"=>"55874249600"}, {"first_name"=>"Tânia Filipa", "last_name"=>"Oliveira", "scopus_author_id"=>"15729975800"}, {"first_name"=>"Przemyslaw", "last_name"=>"Nogly", "scopus_author_id"=>"15136648600"}, {"first_name"=>"Miguel", "last_name"=>"Pessanha", "scopus_author_id"=>"6603570426"}, {"first_name"=>"Meike", "last_name"=>"Stelter", "scopus_author_id"=>"6603849270"}, {"first_name"=>"Arnulf", "last_name"=>"Kletzin", "scopus_author_id"=>"55971298300"}, {"first_name"=>"Peter J.F.", "last_name"=>"Henderson", "scopus_author_id"=>"35765334500"}, {"first_name"=>"Margarida", "last_name"=>"Archer", "scopus_author_id"=>"7102488457"}], "year"=>2013, "source"=>"PLoS ONE", "identifiers"=>{"issn"=>"19326203", "scopus"=>"2-s2.0-84885028668", "sgr"=>"84885028668", "pui"=>"369965583", "isbn"=>"1932-6203", "pmid"=>"24282478", "doi"=>"10.1371/journal.pone.0076913"}, "id"=>"9248f4ee-ad46-3a62-ab42-361bf29cc9e4", "abstract"=>"BACKGROUND: Membrane proteins play a key role in many fundamental cellular processes such as transport of nutrients, sensing of environmental signals and energy transduction, and account for over 50% of all known drug targets. Despite their importance, structural and functional characterisation of membrane proteins still remains a challenge, partially due to the difficulties in recombinant expression and purification. Therefore the need for development of efficient methods for heterologous production is essential.\\n\\nMETHODOLOGY/PRINCIPAL FINDINGS: Fifteen integral membrane transport proteins from Archaea were selected as test targets, chosen to represent two superfamilies widespread in all organisms known as the Major Facilitator Superfamily (MFS) and the 5-Helix Inverted Repeat Transporter superfamily (5HIRT). These proteins typically have eleven to twelve predicted transmembrane helices and are putative transporters for sugar, metabolite, nucleobase, vitamin or neurotransmitter. They include a wide range of examples from the following families: Metabolite-H(+)-symporter; Sugar Porter; Nucleobase-Cation-Symporter-1; Nucleobase-Cation-Symporter-2; and neurotransmitter-sodium-symporter. Overproduction of transporters was evaluated with three vectors (pTTQ18, pET52b, pWarf) and two Escherichia coli strains (BL21 Star and C43 (DE3)). Thirteen transporter genes were successfully expressed; only two did not express in any of the tested vector-strain combinations. Initial trials showed that seven transporters could be purified and six of these yielded quantities of ≥ 0.4 mg per litre suitable for functional and structural studies. Size-exclusion chromatography confirmed that two purified transporters were almost homogeneous while four others were shown to be non-aggregating, indicating that they are ready for up-scale production and crystallisation trials.\\n\\nCONCLUSIONS/SIGNIFICANCE: Here, we describe an efficient strategy for heterologous production of membrane transport proteins in E. coli. Small-volume cultures (10 mL) produced sufficient amount of proteins to assess their purity and aggregation state. The methods described in this work are simple to implement and can be easily applied to many more membrane proteins.", "link"=>"http://www.mendeley.com/research/efficient-strategy-smallscale-screening-production-archaeal-membrane-transport-proteins-escherichia", "reader_count"=>30, "reader_count_by_academic_status"=>{"Unspecified"=>2, "Professor > Associate Professor"=>1, "Researcher"=>5, "Student > Doctoral Student"=>3, "Student > Ph. D. Student"=>7, "Student > Master"=>4, "Other"=>1, "Student > Bachelor"=>5, "Lecturer"=>1, "Professor"=>1}, "reader_count_by_user_role"=>{"Unspecified"=>2, "Professor > Associate Professor"=>1, "Researcher"=>5, "Student > Doctoral Student"=>3, "Student > Ph. D. 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Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/1226741", "https://ndownloader.figshare.com/files/1226742", "https://ndownloader.figshare.com/files/1226743", "https://ndownloader.figshare.com/files/1226744", "https://ndownloader.figshare.com/files/1226745", "https://ndownloader.figshare.com/files/1226746"], "description"=>"<div><p>Background</p><p>Membrane proteins play a key role in many fundamental cellular processes such as transport of nutrients, sensing of environmental signals and energy transduction, and account for over 50% of all known drug targets. Despite their importance, structural and functional characterisation of membrane proteins still remains a challenge, partially due to the difficulties in recombinant expression and purification. Therefore the need for development of efficient methods for heterologous production is essential.</p> <p>Methodology/Principal Findings</p><p>Fifteen integral membrane transport proteins from Archaea were selected as test targets, chosen to represent two superfamilies widespread in all organisms known as the Major Facilitator Superfamily (MFS) and the 5-Helix Inverted Repeat Transporter superfamily (5HIRT). These proteins typically have eleven to twelve predicted transmembrane helices and are putative transporters for sugar, metabolite, nucleobase, vitamin or neurotransmitter. They include a wide range of examples from the following families: Metabolite-H<sup>+</sup>-symporter; Sugar Porter; Nucleobase-Cation-Symporter-1; Nucleobase-Cation-Symporter-2; and neurotransmitter-sodium-symporter. Overproduction of transporters was evaluated with three vectors (pTTQ18, pET52b, pWarf) and two <i>Escherichia coli</i> strains (BL21 Star and C43 (DE3)). Thirteen transporter genes were successfully expressed; only two did not express in any of the tested vector-strain combinations. Initial trials showed that seven transporters could be purified and six of these yielded quantities of ≥ 0.4 mg per litre suitable for functional and structural studies. Size-exclusion chromatography confirmed that two purified transporters were almost homogeneous while four others were shown to be non-aggregating, indicating that they are ready for up-scale production and crystallisation trials.</p> <p>Conclusions/Significance</p><p>Here, we describe an efficient strategy for heterologous production of membrane transport proteins in <i>E. coli</i>. Small-volume cultures (10 mL) produced sufficient amount of proteins to assess their purity and aggregation state. The methods described in this work are simple to implement and can be easily applied to many more membrane proteins.</p> </div>", "links"=>[], "tags"=>["small-scale", "archaeal", "membrane", "proteins"], "article_id"=>816222, "categories"=>["Biological Sciences"], "users"=>["Pikyee Ma", "Filipa Varela", "Malgorzata Magoch", "Ana Rita Silva", "Ana Lúcia Rosário", "José Brito", "Tânia Filipa Oliveira", "Przemyslaw Nogly", "Miguel Pessanha", "Meike Stelter", "Arnulf Kletzin", "Peter J. F. Henderson", "Margarida Archer"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0076913.s001", "https://dx.doi.org/10.1371/journal.pone.0076913.s002", "https://dx.doi.org/10.1371/journal.pone.0076913.s003", "https://dx.doi.org/10.1371/journal.pone.0076913.s004", "https://dx.doi.org/10.1371/journal.pone.0076913.s005", "https://dx.doi.org/10.1371/journal.pone.0076913.s006"], "stats"=>{"downloads"=>0, "page_views"=>13, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/An_Efficient_Strategy_for_Small_Scale_Screening_and_Production_of_Archaeal_Membrane_Transport_Proteins_in_Escherichia_coli_/816222", "title"=>"An Efficient Strategy for Small-Scale Screening and Production of Archaeal Membrane Transport Proteins in <i>Escherichia coli</i>", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2013-10-07 01:47:36"}
  • {"files"=>["https://ndownloader.figshare.com/files/1226732"], "description"=>"<p>(<b>A</b>) Protein purification by Ni-NTA chromatography of 13 constructs expressed in <i>E. coli</i> BL21 Star. SDS-PAGE (top panel) and Western blot (bottom panel) of purified protein. MW - Bio-rad precision plus protein standards. (<b>B</b>) Estimated protein yield per litre of cell culture after initial Ni-NTA affinity chromatography. N/D - not determined.</p>", "links"=>[], "tags"=>["purification", "membrane"], "article_id"=>816213, "categories"=>["Biological Sciences"], "users"=>["Pikyee Ma", "Filipa Varela", "Malgorzata Magoch", "Ana Rita Silva", "Ana Lúcia Rosário", "José Brito", "Tânia Filipa Oliveira", "Przemyslaw Nogly", "Miguel Pessanha", "Meike Stelter", "Arnulf Kletzin", "Peter J. F. Henderson", "Margarida Archer"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0076913.g005", "stats"=>{"downloads"=>1, "page_views"=>14, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Affinity_purification_of_seven_membrane_transport_proteins_/816213", "title"=>"Affinity purification of seven membrane transport proteins.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-10-07 01:47:36"}
  • {"files"=>["https://ndownloader.figshare.com/files/1226731"], "description"=>"<p>Expression tests of archaeal transporters were performed in <i>E. coli</i> C43(DE3) and BL21 Star strains. Cells were grown in LB medium, induced with 0.5 mM IPTG at OD<sub>600nm</sub> of 0.4-0.8 and harvested 3 hours post-induction. The bars show the OD<sub>600nm</sub> at the time of induction (white) and harvesting (black).</p>", "links"=>[], "tags"=>["induction"], "article_id"=>816212, "categories"=>["Biological Sciences"], "users"=>["Pikyee Ma", "Filipa Varela", "Malgorzata Magoch", "Ana Rita Silva", "Ana Lúcia Rosário", "José Brito", "Tânia Filipa Oliveira", "Przemyslaw Nogly", "Miguel Pessanha", "Meike Stelter", "Arnulf Kletzin", "Peter J. F. Henderson", "Margarida Archer"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0076913.g004", "stats"=>{"downloads"=>1, "page_views"=>18, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Cell_density_at_induction_and_harvesting_/816212", "title"=>"Cell density at induction and harvesting.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-10-07 01:47:36"}
  • {"files"=>["https://ndownloader.figshare.com/files/1226727"], "description"=>"<p>Membrane transport protein genes cloned into pTTQ18, pET52b and pWarf were tested in two <i>E. coli</i> host strains, C43(DE3) and BL21 Star. Membranes were analysed by SDS-PAGE. C - C43(DE3), S - BL21 Star, 1 - pTTQ18, 2 - pET52b(+), 3 - pWarf(-). Positions of the His-tagged protein determined by Western blotting (see <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0076913#pone-0076913-g003\" target=\"_blank\">Figure 3</a>) are indicated by: triangle - protein detected by Western blotting but not visible on SDS-PAGE; star - protein detected by Western blotting and visible on SDS-PAGE gels.</p>", "links"=>[], "tags"=>["archaeal", "membrane", "proteins"], "article_id"=>816208, "categories"=>["Biological Sciences"], "users"=>["Pikyee Ma", "Filipa Varela", "Malgorzata Magoch", "Ana Rita Silva", "Ana Lúcia Rosário", "José Brito", "Tânia Filipa Oliveira", "Przemyslaw Nogly", "Miguel Pessanha", "Meike Stelter", "Arnulf Kletzin", "Peter J. F. Henderson", "Margarida Archer"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0076913.g002", "stats"=>{"downloads"=>2, "page_views"=>23, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_SDS_PAGE_analysis_of_archaeal_membrane_transport_proteins_in_E_coli_membranes_/816208", "title"=>"SDS-PAGE analysis of archaeal membrane transport proteins in <i>E. coli</i> membranes.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-10-07 01:47:36"}
  • {"files"=>["https://ndownloader.figshare.com/files/1226725"], "description"=>"<p>Additional affinity tags and GFP provided by the vector backbone are colour-coded. Protease cleavage sites are indicated by red arrows.</p>", "links"=>[], "tags"=>["constructs", "overexpression"], "article_id"=>816206, "categories"=>["Biological Sciences"], "users"=>["Pikyee Ma", "Filipa Varela", "Malgorzata Magoch", "Ana Rita Silva", "Ana Lúcia Rosário", "José Brito", "Tânia Filipa Oliveira", "Przemyslaw Nogly", "Miguel Pessanha", "Meike Stelter", "Arnulf Kletzin", "Peter J. F. Henderson", "Margarida Archer"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0076913.g001", "stats"=>{"downloads"=>0, "page_views"=>15, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Schematic_representation_of_the_protein_constructs_from_overexpression_in_the_different_vectors_/816206", "title"=>"Schematic representation of the protein constructs from overexpression in the different vectors.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-10-07 01:47:36"}
  • {"files"=>["https://ndownloader.figshare.com/files/1226736"], "description"=>"<p>Target proteins are selected and cloned into expression vectors. A small-scale expression test is performed, followed by a membrane preparation for purification using Ni-NTA affinity chromatography. Affinity purified proteins were subjected to a homogeneity test. The workflow of (blue), success rates (brown) and results (green) are shown.</p>", "links"=>[], "tags"=>["small-scale", "membrane"], "article_id"=>816217, "categories"=>["Biological Sciences"], "users"=>["Pikyee Ma", "Filipa Varela", "Malgorzata Magoch", "Ana Rita Silva", "Ana Lúcia Rosário", "José Brito", "Tânia Filipa Oliveira", "Przemyslaw Nogly", "Miguel Pessanha", "Meike Stelter", "Arnulf Kletzin", "Peter J. F. Henderson", "Margarida Archer"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0076913.g007", "stats"=>{"downloads"=>0, "page_views"=>15, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Summary_of_small_scale_production_of_membrane_proteins_/816217", "title"=>"Summary of small-scale production of membrane proteins.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-10-07 01:47:36"}
  • {"files"=>["https://ndownloader.figshare.com/files/1226734"], "description"=>"<p>The affinity-purified proteins were subjected to size-exclusion chromatography on a Superdex 200 5/150 GL column. The elution profile is shown (top panel). The void volume was 1.07 mL determined with Blue dextran. Samples (30 µL) from the elution fractions were analysed on a 15% SDS-PAGE gel stained with SilverXpress silver staining kit (bottom panel). The arrow indicates position of the target protein.</p>", "links"=>[], "tags"=>["chromatography", "affinity-purified"], "article_id"=>816215, "categories"=>["Biological Sciences"], "users"=>["Pikyee Ma", "Filipa Varela", "Malgorzata Magoch", "Ana Rita Silva", "Ana Lúcia Rosário", "José Brito", "Tânia Filipa Oliveira", "Przemyslaw Nogly", "Miguel Pessanha", "Meike Stelter", "Arnulf Kletzin", "Peter J. F. Henderson", "Margarida Archer"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0076913.g006", "stats"=>{"downloads"=>4, "page_views"=>28, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Size_exclusion_chromatography_of_affinity_purified_proteins_/816215", "title"=>"Size-exclusion chromatography of affinity-purified proteins.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-10-07 01:47:36"}
  • {"files"=>["https://ndownloader.figshare.com/files/1226729"], "description"=>"<p>Membrane transport protein genes cloned into pTTQ18, pET52b and pWarf were tested in two <i>E. coli</i> host strains, C43(DE3) and BL21 Star. Membranes were analysed Western blotting. C - C43(DE3), S - BL21 Star, 1 - pTTQ18, 2 - pET52b(+), 3 - pWarf(-).</p>", "links"=>[], "tags"=>["blot", "archaeal", "membrane", "proteins"], "article_id"=>816210, "categories"=>["Biological Sciences"], "users"=>["Pikyee Ma", "Filipa Varela", "Malgorzata Magoch", "Ana Rita Silva", "Ana Lúcia Rosário", "José Brito", "Tânia Filipa Oliveira", "Przemyslaw Nogly", "Miguel Pessanha", "Meike Stelter", "Arnulf Kletzin", "Peter J. F. Henderson", "Margarida Archer"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0076913.g003", "stats"=>{"downloads"=>3, "page_views"=>15, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Western_blot_analysis_of_archaeal_membrane_transport_proteins_in_E_coli_membranes_/816210", "title"=>"Western blot analysis of archaeal membrane transport proteins in <i>E. coli</i> membranes.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-10-07 01:47:36"}

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Relative Metric

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