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rna polymerase core enzyme  (New England Biolabs)


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    New England Biolabs rna polymerase core enzyme
    Rna Polymerase Core Enzyme, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 89 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/e+coli+rna+polymerase+core+enzyme/E%2Ecoli+RNA+Pol%2C+Core+Enzyme/pm42003578-163-0-7
    Average 95 stars, based on 89 article reviews
    rna polymerase core enzyme - by Bioz Stars, 2026-10
    95/100 stars

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    Related Articles

    Binding Assay:

    Article Title: Type IV secretion system effector sabotages multiple defense systems in a competing bacterium.
    Article Snippet: Effector proteins secreted by bacteria that infect mammalian and plant cells often subdue eukaryotic host cell defenses by simultaneously affecting multiple targets.. However, instances when a bacterial effector injected in the competing bacteria sabotage more than a single target have not been reported.. Here, we demonstrate that the effector protein, LtaE, translocated by the type IV secretion system from the soil bacterium Lysobacter enzymogenes into the competing bacterium, Pseudomonas protegens, affects several targets, thus disabling the antibacterial defenses of the competitor.

    Article Title: LIC_12757 from the pathogenic spirochaete Leptospira interrogans encodes an autoregulated ECF σ E -type factor.
    Article Snippet: .. Reactions containing 33 nM E. coli RNA polymerase core enzyme (New England Biolabs) and increasing concentrations of purified LIC_12757 (0–32 fold excess over core) were assembled in a binding buffer (50 mM NaCl, 10 mM Tris-Cl pH 7.5, 10 mM MgCl2, 10 mM β-mercaptoethanol, and 10 μg/mL BSA, 2.5 % glycerol) in final volumes of 20 μl and incubated for 20 min at 37 ◦C to allow reconstitution of the holoenzyme. ..

    Article Title: Type IV secretion system effector sabotages multiple defense systems in a competing bacterium.
    Article Snippet: For the competitive LuxR binding assay involving LtaE and E. coli RNA polymerase core enzyme (NEB), the LuxR1-His protein was labeled with RED-TrisNTA dye (MO-L018).

    Article Title: Type IV secretion system effector sabotages multiple defense systems in a competing bacterium
    Article Snippet: .. For the competitive LuxR binding assay involving LtaE and E. coli RNA polymerase core enzyme (NEB), the LuxR1-His protein was labeled with RED-Tris-NTA dye (MO-L018). ..

    Labeling:

    Article Title: Type IV secretion system effector sabotages multiple defense systems in a competing bacterium.
    Article Snippet: Effector proteins secreted by bacteria that infect mammalian and plant cells often subdue eukaryotic host cell defenses by simultaneously affecting multiple targets.. However, instances when a bacterial effector injected in the competing bacteria sabotage more than a single target have not been reported.. Here, we demonstrate that the effector protein, LtaE, translocated by the type IV secretion system from the soil bacterium Lysobacter enzymogenes into the competing bacterium, Pseudomonas protegens, affects several targets, thus disabling the antibacterial defenses of the competitor.

    Article Title: Type IV secretion system effector sabotages multiple defense systems in a competing bacterium.
    Article Snippet: For the competitive LuxR binding assay involving LtaE and E. coli RNA polymerase core enzyme (NEB), the LuxR1-His protein was labeled with RED-TrisNTA dye (MO-L018).

    Article Title: Type IV secretion system effector sabotages multiple defense systems in a competing bacterium
    Article Snippet: .. For the competitive LuxR binding assay involving LtaE and E. coli RNA polymerase core enzyme (NEB), the LuxR1-His protein was labeled with RED-Tris-NTA dye (MO-L018). ..

    Purification:

    Article Title: LIC_12757 from the pathogenic spirochaete Leptospira interrogans encodes an autoregulated ECF σ E -type factor.
    Article Snippet: .. Reactions containing 33 nM E. coli RNA polymerase core enzyme (New England Biolabs) and increasing concentrations of purified LIC_12757 (0–32 fold excess over core) were assembled in a binding buffer (50 mM NaCl, 10 mM Tris-Cl pH 7.5, 10 mM MgCl2, 10 mM β-mercaptoethanol, and 10 μg/mL BSA, 2.5 % glycerol) in final volumes of 20 μl and incubated for 20 min at 37 ◦C to allow reconstitution of the holoenzyme. ..

    Incubation:

    Article Title: LIC_12757 from the pathogenic spirochaete Leptospira interrogans encodes an autoregulated ECF σ E -type factor.
    Article Snippet: .. Reactions containing 33 nM E. coli RNA polymerase core enzyme (New England Biolabs) and increasing concentrations of purified LIC_12757 (0–32 fold excess over core) were assembled in a binding buffer (50 mM NaCl, 10 mM Tris-Cl pH 7.5, 10 mM MgCl2, 10 mM β-mercaptoethanol, and 10 μg/mL BSA, 2.5 % glycerol) in final volumes of 20 μl and incubated for 20 min at 37 ◦C to allow reconstitution of the holoenzyme. ..



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    Several RNAs transcribed by the sibD minimal promoter from <t>E.</t> <t>coli</t> chromosomal DNA could be NAD capped. ( A ) Schematic illustration of gene editing designs in the E. coli genome for four small RNAs expression driven by the sibD minimal promoter. The gene body of trpT is highlighted in purple, sroC in green, and ryjA and symR in blue. The sibD minimal promoter ( sibD P-35 ) is labelled as a short red line, and the rrnB terminator is highlighted in yellow. ( B ) Detection of NAD caps in SibD, TrpT, RyjA, SroC, and SymR RNAs with NADbio-northern blotting in the wild-type and indicated mutant strains. ‘ADPRC+’ indicates the biotinylation of NAD-RNAs via the ADPRC-SPAAC reaction with sufficient ADPRC, while ‘ADPRC−’ denotes the ADPRC-SPAAC reaction without ADPRC. 5S RNAs were detected as loading controls. ( C ) Detection and quantification of NAD-RNAs from SibD, TrpT, RyjA, SroC, and SymR using APB gel blotting. Capping ratios were calculated based on the band intensity of the capped transcripts relative to the total transcripts (both capped and uncapped transcripts) in the APB gel.
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    Image Search Results


    Several RNAs transcribed by the sibD minimal promoter from E. coli chromosomal DNA could be NAD capped. ( A ) Schematic illustration of gene editing designs in the E. coli genome for four small RNAs expression driven by the sibD minimal promoter. The gene body of trpT is highlighted in purple, sroC in green, and ryjA and symR in blue. The sibD minimal promoter ( sibD P-35 ) is labelled as a short red line, and the rrnB terminator is highlighted in yellow. ( B ) Detection of NAD caps in SibD, TrpT, RyjA, SroC, and SymR RNAs with NADbio-northern blotting in the wild-type and indicated mutant strains. ‘ADPRC+’ indicates the biotinylation of NAD-RNAs via the ADPRC-SPAAC reaction with sufficient ADPRC, while ‘ADPRC−’ denotes the ADPRC-SPAAC reaction without ADPRC. 5S RNAs were detected as loading controls. ( C ) Detection and quantification of NAD-RNAs from SibD, TrpT, RyjA, SroC, and SymR using APB gel blotting. Capping ratios were calculated based on the band intensity of the capped transcripts relative to the total transcripts (both capped and uncapped transcripts) in the APB gel.

    Journal: Nucleic Acids Research

    Article Title: NAD + capping of sibD transcripts in E. coli is mediated by its minimal promoter and enhanced by ppGpp

    doi: 10.1093/nar/gkag102

    Figure Lengend Snippet: Several RNAs transcribed by the sibD minimal promoter from E. coli chromosomal DNA could be NAD capped. ( A ) Schematic illustration of gene editing designs in the E. coli genome for four small RNAs expression driven by the sibD minimal promoter. The gene body of trpT is highlighted in purple, sroC in green, and ryjA and symR in blue. The sibD minimal promoter ( sibD P-35 ) is labelled as a short red line, and the rrnB terminator is highlighted in yellow. ( B ) Detection of NAD caps in SibD, TrpT, RyjA, SroC, and SymR RNAs with NADbio-northern blotting in the wild-type and indicated mutant strains. ‘ADPRC+’ indicates the biotinylation of NAD-RNAs via the ADPRC-SPAAC reaction with sufficient ADPRC, while ‘ADPRC−’ denotes the ADPRC-SPAAC reaction without ADPRC. 5S RNAs were detected as loading controls. ( C ) Detection and quantification of NAD-RNAs from SibD, TrpT, RyjA, SroC, and SymR using APB gel blotting. Capping ratios were calculated based on the band intensity of the capped transcripts relative to the total transcripts (both capped and uncapped transcripts) in the APB gel.

    Article Snippet: To perform IVT assays with various sigma factors, a similar assay was conducted, except the E. coli RNAP holoenzyme was replaced by the same amount of E. coli RNAP core enzyme (NEB) and in the absence of ppGpp or DksA.

    Techniques: Expressing, Northern Blot, Mutagenesis

    Effects of (p)ppGpp and DksA on transcription and NAD capping of certain small RNAs in E. coli cells. ( A ) The NAD capping level of SibD increased upon transient induction of RelA 455aa and DksA. Both RelA 455aa and DksA were expressed from plasmids under the control of the pBAD promoter. NAD capping of SibD was assessed by APB gel blotting. The total level of SibD RNA in each lane was quantified from the normal gel using ImageJ software and normalized to the intensity in the first EV lane. The NAD capping ratio was calculated as the percentage of the intensity of the NAD-capped band relative to the sum of the intensities of both the capped and uncapped bands in the APB gel. ‘Arabinose−’ indicates RNA samples without arabinose induction, while ‘Arabinose+’ signifies that arabinose was added to induce the expression of RelA 455aa and DksA. ‘EV’ indicates strain carrying the empty pBAD33.1 vector. The tmRNA was used as a loading control and each blotting has three independent replicates. ( B ) Detection of NAD-capped transcripts of five sRNAs with NADbio-northern blotting analysis, including four known NAD-RNAs: SibC, SibD, SibE, and GcvB. The tmRNA was used as a loading control. ( C – G ) Detection of total transcripts and NAD-capped transcripts of five sRNAs, namely SibA, SibC, SibD, SibE, and GcvB, respectively. The total abundance of individual RNA was determined by electrophoresis on a standard PAGE gel followed by northern blotting (labelled as normal gel), while the NAD-capped transcripts were identified with APB gel blotting (labelled as APB gel). The non-NAD-RNA SibA was included as a negative control. The NAD capping ratio was calculated based on the band intensity of the NAD-capped version relative to the total transcription levels (NAD-capped version plus uncapped version). Two types of synthetic RNAs for each sRNA, namely with 5′-ppp- and 5′-NAD modifications, were used as controls.

    Journal: Nucleic Acids Research

    Article Title: NAD + capping of sibD transcripts in E. coli is mediated by its minimal promoter and enhanced by ppGpp

    doi: 10.1093/nar/gkag102

    Figure Lengend Snippet: Effects of (p)ppGpp and DksA on transcription and NAD capping of certain small RNAs in E. coli cells. ( A ) The NAD capping level of SibD increased upon transient induction of RelA 455aa and DksA. Both RelA 455aa and DksA were expressed from plasmids under the control of the pBAD promoter. NAD capping of SibD was assessed by APB gel blotting. The total level of SibD RNA in each lane was quantified from the normal gel using ImageJ software and normalized to the intensity in the first EV lane. The NAD capping ratio was calculated as the percentage of the intensity of the NAD-capped band relative to the sum of the intensities of both the capped and uncapped bands in the APB gel. ‘Arabinose−’ indicates RNA samples without arabinose induction, while ‘Arabinose+’ signifies that arabinose was added to induce the expression of RelA 455aa and DksA. ‘EV’ indicates strain carrying the empty pBAD33.1 vector. The tmRNA was used as a loading control and each blotting has three independent replicates. ( B ) Detection of NAD-capped transcripts of five sRNAs with NADbio-northern blotting analysis, including four known NAD-RNAs: SibC, SibD, SibE, and GcvB. The tmRNA was used as a loading control. ( C – G ) Detection of total transcripts and NAD-capped transcripts of five sRNAs, namely SibA, SibC, SibD, SibE, and GcvB, respectively. The total abundance of individual RNA was determined by electrophoresis on a standard PAGE gel followed by northern blotting (labelled as normal gel), while the NAD-capped transcripts were identified with APB gel blotting (labelled as APB gel). The non-NAD-RNA SibA was included as a negative control. The NAD capping ratio was calculated based on the band intensity of the NAD-capped version relative to the total transcription levels (NAD-capped version plus uncapped version). Two types of synthetic RNAs for each sRNA, namely with 5′-ppp- and 5′-NAD modifications, were used as controls.

    Article Snippet: To perform IVT assays with various sigma factors, a similar assay was conducted, except the E. coli RNAP holoenzyme was replaced by the same amount of E. coli RNAP core enzyme (NEB) and in the absence of ppGpp or DksA.

    Techniques: Control, Software, Expressing, Plasmid Preparation, Northern Blot, Electrophoresis, Negative Control