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Figure 2 | BMC Molecular Biology

Figure 2

From: A novel mutant of the Sup35 protein of Saccharomyces cerevisiae defective in translation termination and in GTPase activity still supports cell viability

Figure 2

S. cerevisiae Sup35p is phosphorylated by PKA in vitro. Proteins were incubated with the PKA catalytic subunit and [γ-32P]ATP, submitted to SDS-PAGE, and visualized by autoradiography. (a) Phosphorylation of wild-type Sup35p in the presence of PKA or PKI. (b) Phosphorylation of A and D mutant proteins by PKA. (c) Recognition of the different proteins by a specific PKA-phosphorylated substrate antibody. Wild-type, A or D mutant proteins were phosphorylated or not by PKA before western blotting and detection using a secondary antibody linked to the alkaline phosphatase. (d) Phosphorylation of C-terminal proteins by PKA.

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BMC Molecular Biology

ISSN: 1471-2199

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