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Fbx15 interacts with the transcriptional repressor subunit SsnF without affecting its stability.

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posted on 2016-09-20, 04:30 authored by Bastian Jöhnk, Özgür Bayram, Anja Abelmann, Thorsten Heinekamp, Derek J. Mattern, Axel A. Brakhage, Ilse D. Jacobsen, Oliver Valerius, Gerhard H. Braus

(A) Scheme of a subset of interacting proteins of Fbx15 and SconB based on LC-MS/MS identifications. Shown are presumably nuclear proteins, which are either exclusively found for each F-box protein or which were found for both. Further Fbx15-TAP co-purified proteins included three CSN subunits and the cyclin-dependent kinase NimX. (B) BiFC of Fbx15 and SsnF showed a predominantly cytoplasmic YFP-signal, whereas unphosphorylated Fbx15[S468|9A] interacted with SsnF primarily in the nucleus. (C) Protein stability assays of SsnF-GFP in wild type, Δfbx15 or fbx15 overexpression backgrounds with cultures exposed to cycloheximide (CHX) showed no Fbx15-dependent SsnF stability changes.

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