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. 2016 Jul 18;113(31):E4567–E4576. doi: 10.1073/pnas.1604936113

Fig. S6.

Fig. S6.

WT and engineered ScHAL2. (A) Presence of a surface-exposed Cys349 in the ScHAL2 crystal structure (1KA1), which may explain the redox-sensitive activity observed in Fig. 8B. (B) The WT ScHAL2 and ScHAL2+3C proteins are equally active in vivo when expressed in yeast cells deficient in ScHAL2 (Δhal2) because both proteins complement PAP levels in Δhal2 to similar levels, albeit still about 10-fold higher than WT. Similar results were obtained in two independent experiments.