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  • pbad33  (ATCC)
    93
    ATCC pbad33
    Construction of the ppk1 deletion mutant (Δ ppk1 ) and complemented strain ( Cppk1 ) of EHEC O157:H7. (A) Schematic diagram of the λ red system homologous recombination. (B) The primers of lane 2 and 5 (N-K) were N1-F and Kana-R. The primers of lane 3 and 6 (K-N) were Kana-F and N2-R. The primers of lane 4 and 7 (P1-P2) were PPK-P1 and PPK-P2. (C) Two pairs of primers ( <t>pBAD33-F/R</t> and ppk-F/R ) were used to verify the complemented strain, which produced products of 2092 bp and 2268 bp, respectively. The Cppk1 strain contained both fragments, while WT strain contained only the 2092 bp, and the Δ ppk1 strain contained neither.
    Pbad33, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pbad33/product/ATCC
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    pbad33 - by Bioz Stars, 2022-08
    93/100 stars
      Buy from Supplier

    86
    New England Biolabs pbad33
    Construction of the ppk1 deletion mutant (Δ ppk1 ) and complemented strain ( Cppk1 ) of EHEC O157:H7. (A) Schematic diagram of the λ red system homologous recombination. (B) The primers of lane 2 and 5 (N-K) were N1-F and Kana-R. The primers of lane 3 and 6 (K-N) were Kana-F and N2-R. The primers of lane 4 and 7 (P1-P2) were PPK-P1 and PPK-P2. (C) Two pairs of primers ( <t>pBAD33-F/R</t> and ppk-F/R ) were used to verify the complemented strain, which produced products of 2092 bp and 2268 bp, respectively. The Cppk1 strain contained both fragments, while WT strain contained only the 2092 bp, and the Δ ppk1 strain contained neither.
    Pbad33, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pbad33/product/New England Biolabs
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    pbad33 - by Bioz Stars, 2022-08
    86/100 stars
      Buy from Supplier

    93
    Addgene inc pbad33 1
    Construction of the ppk1 deletion mutant (Δ ppk1 ) and complemented strain ( Cppk1 ) of EHEC O157:H7. (A) Schematic diagram of the λ red system homologous recombination. (B) The primers of lane 2 and 5 (N-K) were N1-F and Kana-R. The primers of lane 3 and 6 (K-N) were Kana-F and N2-R. The primers of lane 4 and 7 (P1-P2) were PPK-P1 and PPK-P2. (C) Two pairs of primers ( <t>pBAD33-F/R</t> and ppk-F/R ) were used to verify the complemented strain, which produced products of 2092 bp and 2268 bp, respectively. The Cppk1 strain contained both fragments, while WT strain contained only the 2092 bp, and the Δ ppk1 strain contained neither.
    Pbad33 1, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pbad33 1/product/Addgene inc
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    pbad33 1 - by Bioz Stars, 2022-08
    93/100 stars
      Buy from Supplier

    Image Search Results


    Construction of the ppk1 deletion mutant (Δ ppk1 ) and complemented strain ( Cppk1 ) of EHEC O157:H7. (A) Schematic diagram of the λ red system homologous recombination. (B) The primers of lane 2 and 5 (N-K) were N1-F and Kana-R. The primers of lane 3 and 6 (K-N) were Kana-F and N2-R. The primers of lane 4 and 7 (P1-P2) were PPK-P1 and PPK-P2. (C) Two pairs of primers ( pBAD33-F/R and ppk-F/R ) were used to verify the complemented strain, which produced products of 2092 bp and 2268 bp, respectively. The Cppk1 strain contained both fragments, while WT strain contained only the 2092 bp, and the Δ ppk1 strain contained neither.

    Journal: Frontiers in Microbiology

    Article Title: Polyphosphate Kinase 1 Is a Pathogenesis Determinant in Enterohemorrhagic Escherichia coli O157:H7

    doi: 10.3389/fmicb.2021.762171

    Figure Lengend Snippet: Construction of the ppk1 deletion mutant (Δ ppk1 ) and complemented strain ( Cppk1 ) of EHEC O157:H7. (A) Schematic diagram of the λ red system homologous recombination. (B) The primers of lane 2 and 5 (N-K) were N1-F and Kana-R. The primers of lane 3 and 6 (K-N) were Kana-F and N2-R. The primers of lane 4 and 7 (P1-P2) were PPK-P1 and PPK-P2. (C) Two pairs of primers ( pBAD33-F/R and ppk-F/R ) were used to verify the complemented strain, which produced products of 2092 bp and 2268 bp, respectively. The Cppk1 strain contained both fragments, while WT strain contained only the 2092 bp, and the Δ ppk1 strain contained neither.

    Article Snippet: LoVo colonic carcinoma cells and DH5α cells with the plasmid pBAD33 (ATCC, 87402) were purchased from ATCC.

    Techniques: Mutagenesis, Homologous Recombination, Produced

    Induction of ItaT in vivo is toxic. ( A ) The killing activity of ItaT in vivo . Overnight cultures of E. coli MG1655 transformed with pBAD33 and pBAD33-ItaT were serially diluted, and the dilutions were spotted on LB agar plates containing 50 μg/ml chloramphenicol supplemented with 0.1% (w/v) arabinose (lower panel) or without arabinose (upper panel). The plates were incubated at 37°C. ( B ) Growth curves of E. coli MG1655 transformed with pBAD33 and pBAD33-ItaT. Induction of ItaT by the addition of 0.1% (w/v) arabinose suppresses the growth of E. coli harboring pBAD33-ItaT in LB containing 50 μg/ml chloramphenicol. When the OD 660 reached 0.2, arabinose was added to the medium and the culture was continued at 37°C. The arrow in the graph indicates the induction of ItaT by arabinose addition.

    Journal: Nucleic Acids Research

    Article Title: Substrate specificities of Escherichia coli ItaT that acetylates aminoacyl-tRNAs

    doi: 10.1093/nar/gkaa487

    Figure Lengend Snippet: Induction of ItaT in vivo is toxic. ( A ) The killing activity of ItaT in vivo . Overnight cultures of E. coli MG1655 transformed with pBAD33 and pBAD33-ItaT were serially diluted, and the dilutions were spotted on LB agar plates containing 50 μg/ml chloramphenicol supplemented with 0.1% (w/v) arabinose (lower panel) or without arabinose (upper panel). The plates were incubated at 37°C. ( B ) Growth curves of E. coli MG1655 transformed with pBAD33 and pBAD33-ItaT. Induction of ItaT by the addition of 0.1% (w/v) arabinose suppresses the growth of E. coli harboring pBAD33-ItaT in LB containing 50 μg/ml chloramphenicol. When the OD 660 reached 0.2, arabinose was added to the medium and the culture was continued at 37°C. The arrow in the graph indicates the induction of ItaT by arabinose addition.

    Article Snippet: In the RNA preparation from control E. coli harboring the empty pBAD33 vector, the molecular masses corresponding to these Ac-aa-A76 molecules (aa: Ile/Leu, Val or Met) were not observed.

    Techniques: In Vivo, Activity Assay, Transformation Assay, Incubation

    Possible aminoacyl moiety binding site in ItaT. ( A ) Superimposition of the structure of ItaT (green) onto that of NatF complexed with the bisubstrate analog, CoA-Ac-MKAV ( 33 ), depicted by a stick model. ( B ) Detailed view of the structure of the active pocket of ItaT complexed with CoA-Ac-MKAV, from the structure of NatF complexed with the analog in (A). For clarity, the structure of NatF was omitted. ( C ) The killing activities of ItaT variants with mutations in Ac-CoA binding sites in vivo , as in Figure 1A . ( D ) Growth curves of E. coli MG1655 transformed pBAD33-ItaT and its variants in (C), in LB containing 50 μg/ml chloramphenicol and 0.1% (w/v) arabinose at 37°C. ( E ) The killing activities of ItaT variants with mutations in the putative aminoacyl moiety binding site in vivo . ( F ) Growth curves of E. coli MG1655 transformed with pBAD33-ItaT and its variants in (E). (G ) The relative acetylation activities of ItaT variants (wild-type ItaT was taken as 1.0) under standard conditions. The reaction mixtures were incubated at 37°C for 1 h. The bars in the graphs are SD of more than three independent experiments.

    Journal: Nucleic Acids Research

    Article Title: Substrate specificities of Escherichia coli ItaT that acetylates aminoacyl-tRNAs

    doi: 10.1093/nar/gkaa487

    Figure Lengend Snippet: Possible aminoacyl moiety binding site in ItaT. ( A ) Superimposition of the structure of ItaT (green) onto that of NatF complexed with the bisubstrate analog, CoA-Ac-MKAV ( 33 ), depicted by a stick model. ( B ) Detailed view of the structure of the active pocket of ItaT complexed with CoA-Ac-MKAV, from the structure of NatF complexed with the analog in (A). For clarity, the structure of NatF was omitted. ( C ) The killing activities of ItaT variants with mutations in Ac-CoA binding sites in vivo , as in Figure 1A . ( D ) Growth curves of E. coli MG1655 transformed pBAD33-ItaT and its variants in (C), in LB containing 50 μg/ml chloramphenicol and 0.1% (w/v) arabinose at 37°C. ( E ) The killing activities of ItaT variants with mutations in the putative aminoacyl moiety binding site in vivo . ( F ) Growth curves of E. coli MG1655 transformed with pBAD33-ItaT and its variants in (E). (G ) The relative acetylation activities of ItaT variants (wild-type ItaT was taken as 1.0) under standard conditions. The reaction mixtures were incubated at 37°C for 1 h. The bars in the graphs are SD of more than three independent experiments.

    Article Snippet: In the RNA preparation from control E. coli harboring the empty pBAD33 vector, the molecular masses corresponding to these Ac-aa-A76 molecules (aa: Ile/Leu, Val or Met) were not observed.

    Techniques: Binding Assay, In Vivo, Transformation Assay, Incubation

    Possible RNA binding region in ItaT. ( A ) Electrostatic potential of the dimer surface of ItaT. The clustered positively charged residues on α1 in one subunit, enclosed in the dotted box, are highlighted on the right. Positively and negatively charged areas are colored blue and red, respectively. ( B ) Electrostatic potential of the AtaT dimer. The positively charged region toward the Ac-CoA binding pocket spans across the dimer interface. tRNA binding model onto the AtaT dimer. ( C ) The killing activity of ItaT variant with L133E mutation in the dimer interface in vivo , as in Figure 1A (upper panel). Growth curves of E. coli MG1655 transformed pBAD33-ItaT and L133E variant, in LB containing 50 μg/ml chloramphenicol and 0.2% (w/v) arabinose at 37°C (lower graph). ( D ) The killing activities of ItaT variants with mutations in the positively charged area in vivo , as in (C) (upper panel). Growth curves of E. coli MG1655 transformed pBAD33-ItaT and its variants in upper panel, as in (C) (lower left graph), and the magnified view (lower right graph). The bars in the graphs are SD of more than three independent experiments.

    Journal: Nucleic Acids Research

    Article Title: Substrate specificities of Escherichia coli ItaT that acetylates aminoacyl-tRNAs

    doi: 10.1093/nar/gkaa487

    Figure Lengend Snippet: Possible RNA binding region in ItaT. ( A ) Electrostatic potential of the dimer surface of ItaT. The clustered positively charged residues on α1 in one subunit, enclosed in the dotted box, are highlighted on the right. Positively and negatively charged areas are colored blue and red, respectively. ( B ) Electrostatic potential of the AtaT dimer. The positively charged region toward the Ac-CoA binding pocket spans across the dimer interface. tRNA binding model onto the AtaT dimer. ( C ) The killing activity of ItaT variant with L133E mutation in the dimer interface in vivo , as in Figure 1A (upper panel). Growth curves of E. coli MG1655 transformed pBAD33-ItaT and L133E variant, in LB containing 50 μg/ml chloramphenicol and 0.2% (w/v) arabinose at 37°C (lower graph). ( D ) The killing activities of ItaT variants with mutations in the positively charged area in vivo , as in (C) (upper panel). Growth curves of E. coli MG1655 transformed pBAD33-ItaT and its variants in upper panel, as in (C) (lower left graph), and the magnified view (lower right graph). The bars in the graphs are SD of more than three independent experiments.

    Article Snippet: In the RNA preparation from control E. coli harboring the empty pBAD33 vector, the molecular masses corresponding to these Ac-aa-A76 molecules (aa: Ile/Leu, Val or Met) were not observed.

    Techniques: RNA Binding Assay, Binding Assay, Activity Assay, Variant Assay, Mutagenesis, In Vivo, Transformation Assay