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. 1996 Dec 10;93(25):14361–14366. doi: 10.1073/pnas.93.25.14361

Table 1.

In vivo activation of PhoB proteins by ′PhoR and ′VanS kinases

Regulator Kinase Bap sp act*
β-galactosidase sp act
No arabinose With arabinose No arabinose With arabinose
PhoBwt None 0.3  ±  0.1 0.3  ±  0.0 6.1  ±  0.2 6.5  ±  0.7
PhoBwt ′PhoR 0.4  ±  0.1 185  ±  3 6.4  ±  0.2 194  ±  7
PhoBwt ′VanS 0.4  ±  0.2 0.3  ±  0.0 6.1  ±  0.4 6.4  ±  0.1
PhoBM17V,E87D ′PhoR 1.2  ±  1.5 516  ±  36 7.5  ±  2.2 968  ±  8
PhoBM17V,E87D ′VanS 0.4  ±  0.2 63.5  ±  1.3 5.7  ±  0.5 53.1  ±  4.4
PhoBM17V,E87D ′VanSH164Q 0.3  ±  0.0 0.7  ±  0.2 6.7  ±  0.2 4.7  ±  0.1
PhoBT97A ′PhoR 0.6  ±  0.0 174  ±  8 6.7  ±  0.1 204  ±  10
PhoBT97A ′VanS 0.4  ±  0.0 125  ±  9 6.4  ±  0.3 127  ±  7

Cells were assayed after growth in 0.06% glycerol Mops 2 mM Pi media without or with arabinose. Bap, bacterial alkaline phosphatase. 

*

Specific activity (sp act) units are nanomoles of product formed per minute per cell optical density at 420 nm. Means of triplicate determinations with standard deviations are given. 

Strains are integrants of BW23316 [like BW23423, except Δ(araBAD)AH37], BW23423, BW23425, or BW23427 with a pSK50 derivative encoding the respective PhoB protein.