Structure of the TXNL1-bound proteasome
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ABSTRACT:
PROVIDER: PRJNA1134194 | ENA |
REPOSITORIES: ENA
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Project description:Proteasomes degrade diverse proteins in different cellular contexts through incompletely defined regulatory mechanisms. Here, we report the cryo-EM structure of thioredoxin-like protein 1 (TXNL1) bound to the 19S regulatory particle of proteasomes via interactions with PSMD1/Rpn2, PSMD4/Rpn10, and PSMD14/Rpn11. Proteasome binding is necessary for the ubiquitin-independent degradation of TXNL1 upon cellular exposure to metal- or metalloid-containing oxidative agents, thereby establishing a structural requirement for the stress-induced degradation of TXNL1.
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2006-02-28 | GSE4272 | GEO
Project description:The proteasome can regulate transcription through proteolytic processing of transcription factors and via gene locus binding, but few targets of proteasomal regulation have been identified. Using genome-wide location analysis and transcriptional profiling in Saccharomyces cerevisiae, we have established which genes are bound and regulated by the proteasome, and by Spt23 and Mga2, transcription factors activated by the proteasome. We observed proteasome association with gene sets that are highly transcribed, controlled by the mating-type loci, and involved in lipid metabolism. At ribosomal protein genes, proteasome and RNA polymerase II binding was enriched in a proteasome mutant, indicating a role for the proteasome in dissociating elongation complexes. The genomic occupancies of Spt23 and Mga2 overlapped significantly with the genes bound by the proteasome. Finally, the proteasome acts in two distinct ways, one dependent and one independent of Spt23/Mga2 cleavage, providing evidence for cooperative gene regulation by the proteasome and its substrates. Keywords: ChIP-chip; genetic modification transcriptional profiling Six genomic localization analysis (GLA, ChIP2) experiments are represented by 18 samples. Six transcriptional profiling experiments (prof) are also represented. Experiments were generally done in triplicate, with fluors swapped on the third replicate.
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