TABLE 4.
Effect of point mutations in licR on β-galactosidase activity of the translational licB′[2530]-lacZ fusiona
| Strainb | Relevant genotypec | β-Galactosidase activity (Miller units) withd:
|
|||
|---|---|---|---|---|---|
| 0.1% ribose | 0.3% glucose | 0.05% cellobiose | 0.1% LHe | ||
| BGT2530b | Wild type | 2.9 | 1.3 | 182 (1.8) | 794 (0.9) |
| BGT2530b1D | licRH219D | 1.3 | 0.6 | 4.6 (0.9) | 3.1 (0.5) |
| BGT2530b1A | licRH219A | 0.8 | 0.3 | 14.9 (0.3) | 37.5 (0.2) |
| BGT2530b2E | licRH278E | 0.7 | 0.2 | 0.9 (0.3) | 1 (0.3) |
| BGT2530b2A | licRH278A | 0.4 | 0.5 | 2.8 (0.7) | 1.4 (0.4) |
| BGT2530b3A | licRH333A | 0.7 | 0.4 | 0.7 (0.3) | 0.9 (0.3) |
| BGT2530b4E | licRH392E | 0.7 | 0.5 | 0.6 (0.3) | 0.8 (0.3) |
| BGT2530b4I | licRH392I | 0.6 | 0.4 | 9.6 (0.5) | 18.8 (0.3) |
| BGT2530b5G | licRH559G | 922 | 16 | 241 (15) | 829 (16) |
a
Growth conditions and sample collection were as described in Table 2, footnote a. Representative results from three independent experiments are shown.
b
See Fig. 1.
c
The position of the histidine residue within LicR exchanged for another amino acid and the designation of the new residue in one-letter code are indicated.
d
Values in parentheses are those when 0.3% glucose was also added.
e
LH, lichenan hydrolysate.