TABLE 2.
Strain | Genotype | Fusiona | β-Galactosidase
activity under the following growth conditionb:
|
|||||||
---|---|---|---|---|---|---|---|---|---|---|
Glc-NH4 | Succ-NH4 | Glc-Asp | Succ-Asp | Glc-Succ-NH4 | Glc-Succ-Asp | Glc-Asp-NH4 | Succ-Asp-NH4 | |||
3841 | Wild type | dctA-lacZ | 266 ± 61 | 2,067 ± 267 | 1,533 ± 356 | 3,433 ± 101 | 2,228 ± 257 | 3,997 ± 273 | 1,944 ± 128 | 1,751 ± 253 |
RU150 | dctA101 | dctA-lacZ | 148 ± 28 | 2,223 ± 120 | 1,251 ± 73 | |||||
RU727 | dctA::Ω | dctA-lacZ | 297 ± 25 | 3,417 ± 248 | 2,073 ± 212 | 3,396 ± 354 | 2,558 ± 341 | |||
RU730 | dctB::Ω | dctA-lacZ | 184 ± 27 | 273 ± 36 | 102 ± 20 | 237 ± 112 | 102 ± 33 | |||
RU711 | dctD::Ω | dctA-lacZ | 150 ± 26 | 235 ± 6 | 91 ± 5 | 198 ± 35 | 136 ± 47 | |||
RU865 | ΔdctBD::Ω | dctA-lacZ | 168 ± 10 | 255 ± 61 | 141 ± 53 | 460 ± 157 | 210 ± 73 | |||
RU714 | ΔdctABD::Ω | dctA-lacZ | 179 ± 65 | 264 ± 46 | 205 ± 50 | 380 ± 122 | 161 ± 35 | |||
RU436 | dctA::Tn5 | dctA-lacZ | 286 ± 12 | 2,945 ± 123 | 2,407 ± 122 | 4,080 ± 147 | 1,886 ± 58 | |||
RU437 | dctA::Tn5 | dctA-lacZ | 230 ± 37 | 3,078 ± 369 | 3,057 ± 107 | 4,475 ± 143 | 2,281 ± 165 | |||
3855 | Wild type | dctA-lacZ | 260 ± 45 | 1,620 ± 75 | 1,960 ± 104 | |||||
CR534 | dctA::Tn5 | dctA-lacZ | 315 ± 85 | 2,755 ± 84 | 3,119 ± 123 | |||||
CR535 | dctB::Tn5 | dctA-lacZ | 113 ± 12 | 95 ± 3 | 97 ± 12 | |||||
CR538 | dctD::Tn5 | dctA-lacZ | 111 ± 21 | 120 ± 12 | 111 ± 23 | |||||
3841 | Wild type | pMP220 | 120 ± 40 | 168 ± 21 | 180 ± 42 | 205 ± 62 |
The dctA-lacZ fusion is pRU103; the vector control is pMP220.
Results are shown as o-nitrophenylgalactoside hydrolyzed (in nanomoles per minute per milligram of protein ± SEM) and are based on at least three independent cultures assayed in triplicate. Glc, glucose; Succ, succinate; Asp, aspartate. All growth substrates were used at 10 mM concentrations.