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purexpress coupled transcription translation system  (New England Biolabs)


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    New England Biolabs purexpress coupled transcription translation system
    Purexpress Coupled Transcription Translation System, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 742 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/purexpress+coupled+transcription+translation+system/PURExpress+In+Vitro+Protein+Synthesis+Kit/pm41565654-273-37-41
    Average 99 stars, based on 742 article reviews
    purexpress coupled transcription translation system - by Bioz Stars, 2026-10
    99/100 stars

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    Related Articles

    Purification:

    Article Title: Phospholipid composition strongly affects the assembly of β barrel proteins into purified bacterial outer membranes.
    Article Snippet: .. AR TI CL E IN P RE SS OMP assembly assays using purified native OMs OMP assembly in vitro was assessed using a modified version of an assay in which OMPs are produced de novo in the PURExpress coupled transcription/translation system (New England Biolabs, catalog number E6800)54. ..

    Article Title: Antibacterial macrocyclic peptides reveal a distinct mode of BamA inhibition
    Article Snippet: .. EspPΔ5′, OmpT and OmpC were synthesized using the PURExpress coupled transcription-translation system (New England Biolabs) according to the manufacturer’s instructions, except that reactions were supplemented with 2 μM purified SurA and sonicated proteoliposomes containing purified BAM (0.5 μM) and 1-palmitoyl-2-oleoyl-glycero-3-phosphocholine (POPC). .. Typical 10 μL reactions also contained murine RNAse Inhibitor (8 U) and 0.4 μM FluoroTect GreenLys (Promega), a lysine-charged tRNA labeled with the fluorophore BODIPY-FL at the ε position that was used to introduce fluorescent lysine residues into each OMP during translation.

    Article Title: Antibacterial macrocyclic peptides reveal a distinct mode of BamA inhibition.
    Article Snippet: .. EspPΔ5′, OmpT and OmpC were synthesized using the PURExpress coupled transcription-translation system (New England Biolabs) according to the manufacturer’s instructions, except that reactions were supplemented with 2 μM purified SurA and sonicated proteoliposomes containing purified BAM (0.5 μM) and 1- palmitoyl-2-oleoyl-glycero-3-phosphocholine (POPC). .. Typical 10μL reactions also contained murine RNAse Inhibitor (8 U) and 0.4μM FluoroTect GreenLys (Promega), a lysine-charged tRNA labeled with the fluorophore BODIPY-FL at the ε position that was used to introduce fluorescent lysine residues into each OMP during translation.

    In Vitro:

    Article Title: Phospholipid composition strongly affects the assembly of β barrel proteins into purified bacterial outer membranes.
    Article Snippet: .. AR TI CL E IN P RE SS OMP assembly assays using purified native OMs OMP assembly in vitro was assessed using a modified version of an assay in which OMPs are produced de novo in the PURExpress coupled transcription/translation system (New England Biolabs, catalog number E6800)54. ..

    Modification:

    Article Title: Phospholipid composition strongly affects the assembly of β barrel proteins into purified bacterial outer membranes.
    Article Snippet: .. AR TI CL E IN P RE SS OMP assembly assays using purified native OMs OMP assembly in vitro was assessed using a modified version of an assay in which OMPs are produced de novo in the PURExpress coupled transcription/translation system (New England Biolabs, catalog number E6800)54. ..

    Produced:

    Article Title: Phospholipid composition strongly affects the assembly of β barrel proteins into purified bacterial outer membranes.
    Article Snippet: .. AR TI CL E IN P RE SS OMP assembly assays using purified native OMs OMP assembly in vitro was assessed using a modified version of an assay in which OMPs are produced de novo in the PURExpress coupled transcription/translation system (New England Biolabs, catalog number E6800)54. ..

    Synthesized:

    Article Title: The translocation assembly module (TAM) catalyzes the assembly of bacterial outer membrane proteins in vitro
    Article Snippet: .. The data show that the PK-resistance patterns of Ag43-β assembled into TAM/PLE and TamA/PLE proteoliposomes were similar. d FadL was synthesized de novo in the PURExpress coupled transcription/translation system (New England BioLabs, catalog number E6800L) using the plasmid pET303::fadL26-446. .. The reaction was supplemented with BODIPY-FL-ε-Lys-tRNALys (Promega, catalog number L5001) to fluorescently label FadL, 2 μM SurA and 2 μM Bam/POPC proteoliposomes to analyze BAM-mediated folding of FadL as described previously11.

    Article Title: Reconstitution of Bam Complex-Mediated Assembly of a Trimeric Porin into Proteoliposomes
    Article Snippet: .. In most experiments, OmpC was synthesized using the PURExpress coupled transcription-translation system (New England BioLabs) according to the manufacturer’s instructions. .. Typical 10-μl reaction mixtures (used for single-time-point experiments) contained a murine RNase inhibitor (8 U) and 0.4 μl FluoroTect Green Lys , a lysine-charged tRNA labeled with the fluorophore BODIPY-FL at the ε position (Promega) that was used to incorporate fluorescent lysine residues into OmpC.

    Article Title: Bam complex-mediated assembly of bacterial outer membrane proteins synthesized in an in vitro translation system
    Article Snippet: His-tagged Skp was obtained from MyBioSource. .. OMPs were synthesized using the PURExpress coupled transcription-translation system (New England Biolabs) according to the supplier’s instructions, except that reactions were supplemented with 2 μM SurA (or other chaperone) and pre-sonicated 1-palmitoyl-2-oleoyl-glycero-3-phosphocholine (POPC) proteoliposomes containing the Bam complex (0.5 μM). .. Typical 10 μL reactions (used for single timepoint experiments) also contained murine RNase Inhibitor (8 U) and 0.4 μL FluoroTect Green Lys , a lysine-charged tRNA labeled with the fluorophore BODIPY-FL at the ε position (Promega).

    Article Title: Antibacterial macrocyclic peptides reveal a distinct mode of BamA inhibition
    Article Snippet: .. EspPΔ5′, OmpT and OmpC were synthesized using the PURExpress coupled transcription-translation system (New England Biolabs) according to the manufacturer’s instructions, except that reactions were supplemented with 2 μM purified SurA and sonicated proteoliposomes containing purified BAM (0.5 μM) and 1-palmitoyl-2-oleoyl-glycero-3-phosphocholine (POPC). .. Typical 10 μL reactions also contained murine RNAse Inhibitor (8 U) and 0.4 μM FluoroTect GreenLys (Promega), a lysine-charged tRNA labeled with the fluorophore BODIPY-FL at the ε position that was used to introduce fluorescent lysine residues into each OMP during translation.

    Article Title: Antibacterial macrocyclic peptides reveal a distinct mode of BamA inhibition.
    Article Snippet: .. EspPΔ5′, OmpT and OmpC were synthesized using the PURExpress coupled transcription-translation system (New England Biolabs) according to the manufacturer’s instructions, except that reactions were supplemented with 2 μM purified SurA and sonicated proteoliposomes containing purified BAM (0.5 μM) and 1- palmitoyl-2-oleoyl-glycero-3-phosphocholine (POPC). .. Typical 10μL reactions also contained murine RNAse Inhibitor (8 U) and 0.4μM FluoroTect GreenLys (Promega), a lysine-charged tRNA labeled with the fluorophore BODIPY-FL at the ε position that was used to introduce fluorescent lysine residues into each OMP during translation.

    Article Title: Reconstitution of Bam Complex-Mediated Assembly of a Trimeric Porin into Proteoliposomes
    Article Snippet: .. In most experiments, OmpC was synthesized using the PURExpress coupled transcription-translation system (New England BioLabs) according to the manufacturer’s instructions. .. Typical 10-ml reaction mixtures (used for single-time-point experiments) contained a murine RNase inhibitor (8 U) and 0.4 ml FluoroTect GreenLys, a lysine-charged tRNA labeled with the fluorophore BODIPY-FL at the « position (Promega) that was used to incorporate fluorescent lysine residues into OmpC.

    Plasmid Preparation:

    Article Title: The translocation assembly module (TAM) catalyzes the assembly of bacterial outer membrane proteins in vitro
    Article Snippet: .. The data show that the PK-resistance patterns of Ag43-β assembled into TAM/PLE and TamA/PLE proteoliposomes were similar. d FadL was synthesized de novo in the PURExpress coupled transcription/translation system (New England BioLabs, catalog number E6800L) using the plasmid pET303::fadL26-446. .. The reaction was supplemented with BODIPY-FL-ε-Lys-tRNALys (Promega, catalog number L5001) to fluorescently label FadL, 2 μM SurA and 2 μM Bam/POPC proteoliposomes to analyze BAM-mediated folding of FadL as described previously11.

    Sonication:

    Article Title: Antibacterial macrocyclic peptides reveal a distinct mode of BamA inhibition
    Article Snippet: .. EspPΔ5′, OmpT and OmpC were synthesized using the PURExpress coupled transcription-translation system (New England Biolabs) according to the manufacturer’s instructions, except that reactions were supplemented with 2 μM purified SurA and sonicated proteoliposomes containing purified BAM (0.5 μM) and 1-palmitoyl-2-oleoyl-glycero-3-phosphocholine (POPC). .. Typical 10 μL reactions also contained murine RNAse Inhibitor (8 U) and 0.4 μM FluoroTect GreenLys (Promega), a lysine-charged tRNA labeled with the fluorophore BODIPY-FL at the ε position that was used to introduce fluorescent lysine residues into each OMP during translation.

    Article Title: Antibacterial macrocyclic peptides reveal a distinct mode of BamA inhibition.
    Article Snippet: .. EspPΔ5′, OmpT and OmpC were synthesized using the PURExpress coupled transcription-translation system (New England Biolabs) according to the manufacturer’s instructions, except that reactions were supplemented with 2 μM purified SurA and sonicated proteoliposomes containing purified BAM (0.5 μM) and 1- palmitoyl-2-oleoyl-glycero-3-phosphocholine (POPC). .. Typical 10μL reactions also contained murine RNAse Inhibitor (8 U) and 0.4μM FluoroTect GreenLys (Promega), a lysine-charged tRNA labeled with the fluorophore BODIPY-FL at the ε position that was used to introduce fluorescent lysine residues into each OMP during translation.



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    ( a ) Overview of the structure of the <t>E.</t> <t>coli</t> 70S ribosome stalled by BOT (yellow) during in vitro translation of the dapG mRNA. The 30S and 50S subunits are shown in light yellow and light blue, respectively; EF-Tu is in teal; the mRNA is in blue, and the A-and P-site tRNAs are in dark blue and orange, respectively. BOT traps glycyl-tRNA in complex with EF-Tu on the ribosome in an A/T-state, preventing proper accommodation into the A site. The position of the fully accommodated A/A tRNA is indicated by a black outline. ( b ) Close-up view of the ribosome-bound EF-Tu•GDP•Gly-tRNA ternary complex with BOT bound at the interface between EF-Tu domains I and II (teal and green), adjacent to the CCA-end of the Gly-tRNA (dark blue). GDP (orange) in the GTPase center indicates a post-hydrolysis state of EF-Tu. ( c ) Cryo-EM density map (blue mesh) for BOT with the refined atomic model overlaid. Two orthogonal views reveal well-resolved density for all key chemical moieties of the drug, allowing confident placement and modeling. ( d, e ) Detailed views of the interaction network between BOT, EF-Tu, and the CCA-end of Gly-tRNA. BOT forms an extensive H-bonding interface with EF-Tu domain I (Asn64-Val68), domain II (Asp217 and Arg263) residues, and the phosphate of nucleotide C75. H-bonds are shown as black dotted lines. ( f ) CH-π stacking between the β-methyl-phenylalanine (mPhe) side chain of BOT and the glycine moiety of the aa-tRNA. This highly specific interaction explains the strict selectivity of BOT for glycyl-tRNA and its amino acid-dependent inhibitory activity.
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    ( a ) Overview of the structure of the <t>E.</t> <t>coli</t> 70S ribosome stalled by BOT (yellow) during in vitro translation of the dapG mRNA. The 30S and 50S subunits are shown in light yellow and light blue, respectively; EF-Tu is in teal; the mRNA is in blue, and the A-and P-site tRNAs are in dark blue and orange, respectively. BOT traps glycyl-tRNA in complex with EF-Tu on the ribosome in an A/T-state, preventing proper accommodation into the A site. The position of the fully accommodated A/A tRNA is indicated by a black outline. ( b ) Close-up view of the ribosome-bound EF-Tu•GDP•Gly-tRNA ternary complex with BOT bound at the interface between EF-Tu domains I and II (teal and green), adjacent to the CCA-end of the Gly-tRNA (dark blue). GDP (orange) in the GTPase center indicates a post-hydrolysis state of EF-Tu. ( c ) Cryo-EM density map (blue mesh) for BOT with the refined atomic model overlaid. Two orthogonal views reveal well-resolved density for all key chemical moieties of the drug, allowing confident placement and modeling. ( d, e ) Detailed views of the interaction network between BOT, EF-Tu, and the CCA-end of Gly-tRNA. BOT forms an extensive H-bonding interface with EF-Tu domain I (Asn64-Val68), domain II (Asp217 and Arg263) residues, and the phosphate of nucleotide C75. H-bonds are shown as black dotted lines. ( f ) CH-π stacking between the β-methyl-phenylalanine (mPhe) side chain of BOT and the glycine moiety of the aa-tRNA. This highly specific interaction explains the strict selectivity of BOT for glycyl-tRNA and its amino acid-dependent inhibitory activity.
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    Image Search Results


    ( a ) Overview of the structure of the E. coli 70S ribosome stalled by BOT (yellow) during in vitro translation of the dapG mRNA. The 30S and 50S subunits are shown in light yellow and light blue, respectively; EF-Tu is in teal; the mRNA is in blue, and the A-and P-site tRNAs are in dark blue and orange, respectively. BOT traps glycyl-tRNA in complex with EF-Tu on the ribosome in an A/T-state, preventing proper accommodation into the A site. The position of the fully accommodated A/A tRNA is indicated by a black outline. ( b ) Close-up view of the ribosome-bound EF-Tu•GDP•Gly-tRNA ternary complex with BOT bound at the interface between EF-Tu domains I and II (teal and green), adjacent to the CCA-end of the Gly-tRNA (dark blue). GDP (orange) in the GTPase center indicates a post-hydrolysis state of EF-Tu. ( c ) Cryo-EM density map (blue mesh) for BOT with the refined atomic model overlaid. Two orthogonal views reveal well-resolved density for all key chemical moieties of the drug, allowing confident placement and modeling. ( d, e ) Detailed views of the interaction network between BOT, EF-Tu, and the CCA-end of Gly-tRNA. BOT forms an extensive H-bonding interface with EF-Tu domain I (Asn64-Val68), domain II (Asp217 and Arg263) residues, and the phosphate of nucleotide C75. H-bonds are shown as black dotted lines. ( f ) CH-π stacking between the β-methyl-phenylalanine (mPhe) side chain of BOT and the glycine moiety of the aa-tRNA. This highly specific interaction explains the strict selectivity of BOT for glycyl-tRNA and its amino acid-dependent inhibitory activity.

    Journal: bioRxiv

    Article Title: Sequence-specific trapping of EF-Tu/glycyl-tRNA complex on the ribosome by bottromycin

    doi: 10.1101/2025.08.17.670399

    Figure Lengend Snippet: ( a ) Overview of the structure of the E. coli 70S ribosome stalled by BOT (yellow) during in vitro translation of the dapG mRNA. The 30S and 50S subunits are shown in light yellow and light blue, respectively; EF-Tu is in teal; the mRNA is in blue, and the A-and P-site tRNAs are in dark blue and orange, respectively. BOT traps glycyl-tRNA in complex with EF-Tu on the ribosome in an A/T-state, preventing proper accommodation into the A site. The position of the fully accommodated A/A tRNA is indicated by a black outline. ( b ) Close-up view of the ribosome-bound EF-Tu•GDP•Gly-tRNA ternary complex with BOT bound at the interface between EF-Tu domains I and II (teal and green), adjacent to the CCA-end of the Gly-tRNA (dark blue). GDP (orange) in the GTPase center indicates a post-hydrolysis state of EF-Tu. ( c ) Cryo-EM density map (blue mesh) for BOT with the refined atomic model overlaid. Two orthogonal views reveal well-resolved density for all key chemical moieties of the drug, allowing confident placement and modeling. ( d, e ) Detailed views of the interaction network between BOT, EF-Tu, and the CCA-end of Gly-tRNA. BOT forms an extensive H-bonding interface with EF-Tu domain I (Asn64-Val68), domain II (Asp217 and Arg263) residues, and the phosphate of nucleotide C75. H-bonds are shown as black dotted lines. ( f ) CH-π stacking between the β-methyl-phenylalanine (mPhe) side chain of BOT and the glycine moiety of the aa-tRNA. This highly specific interaction explains the strict selectivity of BOT for glycyl-tRNA and its amino acid-dependent inhibitory activity.

    Article Snippet: Toeprinting analysis was carried out using model mRNA templates listed in and PURExpress E. coli in vitro transcription-translation coupled system (NEB) as described previously .

    Techniques: In Vitro, Cryo-EM Sample Prep, Activity Assay

    ( a ) Characteristics of B. subtilis mutants selected on BOT-containing agar plates. All resistant clones carried point mutations at Asp218 residue in the tuf gene. ( b ) Location of residue Asp218 ( B. subtilis numbering; equivalent to Asp217 in E. coli ) within EF-Tu, mapped onto its domain organization. ( c, d ) In silico modeling of the D217Y ( E. coli numbering) substitution in the structure of EF-Tu/Gly-tRNA/BOT complex reveals a steric clash between the bulky tyrosine side chain and the bound BOT molecule. ( e ) Schematic of engineered B. subtilis strains harboring a second copy of the tuf gene inserted at the chromosomal lacA locus under the control of an xylose-inducible promoter. ( f ) Heat map showing the growth (OD 600 ) of the four strains shown in ( e ) in SM minimal medium supplemented with increasing concentrations of BOT and 1% xylose. ( g ) Growth of the same strains on SM minimal agar plates supplemented with 1% xylose, without the drug (top) or with 2 µg/mL BOT (bottom). ( h ) Distribution of tuf gene paralogs (encoding EF-Tu) across complete bacterial genomes from major classes/phyla. Selected species known to be highly sensitive to BOT are listed in the insets along with their respective tuf copy number.

    Journal: bioRxiv

    Article Title: Sequence-specific trapping of EF-Tu/glycyl-tRNA complex on the ribosome by bottromycin

    doi: 10.1101/2025.08.17.670399

    Figure Lengend Snippet: ( a ) Characteristics of B. subtilis mutants selected on BOT-containing agar plates. All resistant clones carried point mutations at Asp218 residue in the tuf gene. ( b ) Location of residue Asp218 ( B. subtilis numbering; equivalent to Asp217 in E. coli ) within EF-Tu, mapped onto its domain organization. ( c, d ) In silico modeling of the D217Y ( E. coli numbering) substitution in the structure of EF-Tu/Gly-tRNA/BOT complex reveals a steric clash between the bulky tyrosine side chain and the bound BOT molecule. ( e ) Schematic of engineered B. subtilis strains harboring a second copy of the tuf gene inserted at the chromosomal lacA locus under the control of an xylose-inducible promoter. ( f ) Heat map showing the growth (OD 600 ) of the four strains shown in ( e ) in SM minimal medium supplemented with increasing concentrations of BOT and 1% xylose. ( g ) Growth of the same strains on SM minimal agar plates supplemented with 1% xylose, without the drug (top) or with 2 µg/mL BOT (bottom). ( h ) Distribution of tuf gene paralogs (encoding EF-Tu) across complete bacterial genomes from major classes/phyla. Selected species known to be highly sensitive to BOT are listed in the insets along with their respective tuf copy number.

    Article Snippet: Toeprinting analysis was carried out using model mRNA templates listed in and PURExpress E. coli in vitro transcription-translation coupled system (NEB) as described previously .

    Techniques: Clone Assay, Residue, In Silico, Control