Journal:

Article Title: Identification and Genetic Characterization of a Novel Proteinase, PrtR, from the Human Isolate Lactobacillus rhamnosus BGT10

doi: 10.1128/AEM.69.10.5802-5811.2003

Figure Lengend Snippet: Bacterial strains and plasmids used in this study

Article Snippet: Thick lines represent different fragments of the prtR regulatory region, and dashed lines represent deleted regions. table ft1 table-wrap mode="anchored" t5 TABLE 2. caption a7 Transformant β-Glucuronidase activity (mean ± SD) a in: Induction ratio (0.1%/2% Casitone) CDM supplemented with Casitone at: MRS 0.1% 0.5% 1% 2% ATCC 393 T /pEB640 93 ± 44 31 ± 23 8 ± 6 10 ± 5 3 ± 2 9.30 ATCC 393 T /pEB260 181 ± 86 50 ± 13 20 ± 8 14 ± 5 3 ± 1 12.93 ATCC 393 T /pEB471 121 ± 51 54 ± 24 45 ± 34 20 ± 13 15 ± 7 6.05 ATCC 393 T /pEB99 337 ± 167 129 ± 57 75 ± 10 50 ± 14 12 ± 2 6.74 ATCC 393 T /pEB122 0 0 0 0 0 Open in a separate window a Expressed as nanomoles per minute per milligram of protein.

Techniques: Plasmid Preparation

Journal:

Article Title: Identification and Genetic Characterization of a Novel Proteinase, PrtR, from the Human Isolate Lactobacillus rhamnosus BGT10

doi: 10.1128/AEM.69.10.5802-5811.2003

Figure Lengend Snippet: Determination of the prtR transcription start point. (A) Primer extension analysis of the prtR promoter was performed with RNA from L. casei ATCC 393T cells harboring pEB471. (B) L. casei ATCC 393T cells harboring pEB640 (lane 1) and L. rhamnosus BGT10 (lane 2). The sequencing reactions (A, C, G, and T) were performed with the same primers as the corresponding primer extension reactions. The primer extension products are indicated with an arrow. (C) Interpretation of the primer extension results. The putative −35 and −10 prtR promoter haxamers (underlined), the transcription start point (+1, underlined), and the putative ribosome binding site (RBS) (boldface) are shown. The prtR coding sequence is in italic.

Article Snippet: Thick lines represent different fragments of the prtR regulatory region, and dashed lines represent deleted regions. table ft1 table-wrap mode="anchored" t5 TABLE 2. caption a7 Transformant β-Glucuronidase activity (mean ± SD) a in: Induction ratio (0.1%/2% Casitone) CDM supplemented with Casitone at: MRS 0.1% 0.5% 1% 2% ATCC 393 T /pEB640 93 ± 44 31 ± 23 8 ± 6 10 ± 5 3 ± 2 9.30 ATCC 393 T /pEB260 181 ± 86 50 ± 13 20 ± 8 14 ± 5 3 ± 1 12.93 ATCC 393 T /pEB471 121 ± 51 54 ± 24 45 ± 34 20 ± 13 15 ± 7 6.05 ATCC 393 T /pEB99 337 ± 167 129 ± 57 75 ± 10 50 ± 14 12 ± 2 6.74 ATCC 393 T /pEB122 0 0 0 0 0 Open in a separate window a Expressed as nanomoles per minute per milligram of protein.

Techniques: Sequencing, Binding Assay

Journal:

Article Title: Identification and Genetic Characterization of a Novel Proteinase, PrtR, from the Human Isolate Lactobacillus rhamnosus BGT10

doi: 10.1128/AEM.69.10.5802-5811.2003

Figure Lengend Snippet: Expression of the prtR-gusA fusions in CDM supplemented with casitone and in MRS broth

Article Snippet: Thick lines represent different fragments of the prtR regulatory region, and dashed lines represent deleted regions. table ft1 table-wrap mode="anchored" t5 TABLE 2. caption a7 Transformant β-Glucuronidase activity (mean ± SD) a in: Induction ratio (0.1%/2% Casitone) CDM supplemented with Casitone at: MRS 0.1% 0.5% 1% 2% ATCC 393 T /pEB640 93 ± 44 31 ± 23 8 ± 6 10 ± 5 3 ± 2 9.30 ATCC 393 T /pEB260 181 ± 86 50 ± 13 20 ± 8 14 ± 5 3 ± 1 12.93 ATCC 393 T /pEB471 121 ± 51 54 ± 24 45 ± 34 20 ± 13 15 ± 7 6.05 ATCC 393 T /pEB99 337 ± 167 129 ± 57 75 ± 10 50 ± 14 12 ± 2 6.74 ATCC 393 T /pEB122 0 0 0 0 0 Open in a separate window a Expressed as nanomoles per minute per milligram of protein.

Techniques: Expressing, Activity Assay