TABLE 3.
Transcription activation by partially constitutive variants of RhaS with substitutions that map to RhaS-CTD
β-Galactosidase Activityc | ||||
---|---|---|---|---|
Expt | RhaS varianta | No. of isolatesb | (−) L-rhamnose | (+) L-rhamnose |
A | Wild type | 0.55 | 218 | |
F184Y/Q207R | 1 | 8.6 | 8.9 | |
L201R | 6 | 54 | 329 | |
L208F | 2 | 5.6 | 285 | |
Q210R | 1 | 2.6 | 326 | |
B | Wild type | 0.34 | 206 | |
F184Y | 0.69 | 218 | ||
Q207R | 0.73 | 243 |
Wild type and RhaS variants were encoded on pHG165 transformed into SME3000 (λΦ(rhaB-lacZ)Δ84 Δ(rhaSR)::Km).
Number of times this substitution was independently isolated in random mutagenesis screen.
Cultures were grown in MOPS growth medium containing glycerol plus ampicillin with or without L-rhamnose as indicated. β-Galactosidase activity (in Miller Units) was assayed. Standard errors were less than 20% of the average units, except for a few of the samples with activities below 3 Miller units. These had errors up to 31% of the average units.