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Effects of mutation of the SUMO protease Ulp1 on chromatin-associated sumoylation genome-wide in budding yeast

ABSTRACT: Steady-state levels of SUMO post-translational modifications are determined by the balance between sumoylation and desumoylation machineries. Eukaryotic cells can modulate cellular levels of SUMO conjugation by regulating the enzymes involved in these processes. In budding yeast, for example, heat shock induces a global increase in SUMO conjugation, at least in part by triggering the degradation of the major SUMO protease, Ulp1. ChIP-seq analyses by our group and others have identified hundreds of sites across the yeast genome that contain sumoylated proteins, including the promoter regions of 265 protein-coding genes, consistent with a role for sumoylation in regulating transcription widely. Paradoxically, despite the overall increase in SUMO conjugation upon heat shock, chromatin-associated sumoylation decreases at most of these loci when temperatures rise. Here, we show that a similar pattern is observed in a strain expressing a partially defective form of Ulp1, which exhibits constitutively elevated SUMO conjugation yet reduced sumoylation at sites across the genome. One possible explanation is that reduced Ulp1 activity, whether through heat shock-mediated degradation or mutation, indeed elevates sumoylation of chromatin-bound proteins, but this then promotes their rapid dissociation from chromatin. This model aligns with our previous findings that sumoylation triggers the release of the Gcn4 and Sko1 transcription factors from their genomic binding sites.

ORGANISM(S): Saccharomyces cerevisiae

PROVIDER: GSE290843 | GEO | 2026/04/30

REPOSITORIES: GEO

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