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. 2010 Jan 22;192(7):1882–1889. doi: 10.1128/JB.01503-09

TABLE 3.

Two-hybrid assay results

pcI plasmid(s) β-Galactosidase activity (Miller units) Residual β-galactosidase activity (%)
Binding to chimeric operatora
    pcI434 2,350 ± 2.5 95
    pcIP22 2,517 ± 3.4 100
    pcIP22+ pcI434 2,373 ± 1.5 94.1
    pcI434-434 1,886 ± 2.6 75
    pcIP22-434 2,113 ± 3.1 86
    pcI434-434 + pcIP22-434 351 ± 2.7 14
Interaction between RNAPα and RPL2b
    pcIP22-RNAPα 1,915 ± 1.8 76.2
    pcI434-RPL2 1,829 ± 2.5 72.7
    pcI434-RNAPα 2,200 ± 3.4 88
    pcIP22-RNAPα + pcI434-RPL2 880 ± 2.9 35
    pcIP22-RNAPα + pcI434-RNAPα 401 ± 3.2 16
a

The pcI plasmids were inserted into E. coli strain R721 by transformation, and the ability of each reconstituted repressor to bind to the chimeric operator was then determined by measuring the residual β-galactosidase activity.

b

A two-hybrid assay was performed to investigate the interaction between RNAPα and RPL2. Plasmids pcIP22-RNAPα and pcI434-L2 were both expressed in E. coli R721 cells, and the residual β-galactosidase activity was recorded. In the absence of any pcI plasmid, strain R721 produced 2,500 Miller units of β-galactosidase activity (mean of five independent experiments). The values are the means of nine independent experiments.

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