Back to article: The ubiquitin-conjugating enzyme, Ubc1, indirectly regulates SNF1 kinase activity via Forkhead-dependent transcription

FIGURE 3: Snf1 protein abundance, but neither stability nor phosphorylation, is decreased by Ubc1 disruption.

(A) Early logarithmic phase WT and ubc1Δ strains harboring genomic Snf1-GFP were grown in 2% (H) and 0.05% (L) glucose for 1 hour prior to cell lysis, and an equal amount of total protein was loaded in duplicates for Western analysis of total Snf1 (Snf1tot-GFP) and phosphorylated Snf1 (Snf1ph-GFP).

(B) WT and ubc1Δ strains harboring genomic Gal83-TAP or Snf4-TAP were treated as in (A) and Western analysis for TAP abundance is shown.

(C) Assessment of Snf1 protein stability over 3 hours in WT and ubc1Δ strains in the presence of cycloheximide, added at time (0), in 2% glucose. Equal cell numbers were removed at the indicated time points with 40 μg protein loaded.

(D) Biological repeat of Snf1-GFP stability (as in B) is shown with 80 μg protein loaded per lane, and additional timepoints.

By continuing to use the site, you agree to the use of cookies. more information

The cookie settings on this website are set to "allow cookies" to give you the best browsing experience possible. If you continue to use this website without changing your cookie settings or you click "Accept" below then you are consenting to this. Please refer to our "privacy statement" and our "terms of use" for further information.