SUMO Pathway Modulation of Regulatory Protein Binding at the Ribosomal DNA Locus in Saccharomyces cerevisiae

Genetics
Jennifer GilliesMark Hochstrasser

Abstract

In this report, we identify cellular targets of Ulp2, one of two Saccharomyces cerevisiae small ubiquitin-related modifier (SUMO) proteases, and investigate the function of SUMO modification of these proteins. PolySUMO conjugates from ulp2Δ and ulp2Δ slx5Δ cells were isolated using an engineered affinity reagent containing the four SUMO-interacting motifs (SIMs) of Slx5, a component of the Slx5/Slx8 SUMO-targeted ubiquitin ligase (STUbL). Two proteins identified, Net1 and Tof2, regulate ribosomal DNA (rDNA) silencing and were found to be hypersumoylated in ulp2Δ,slx5Δ, and ulp2Δ slx5Δ cells. The increase in sumoylation of Net1 and Tof2 in ulp2Δ, but not ulp1ts cells, indicates that these nucleolar proteins are specific substrates of Ulp2 Based on quantitative chromatin-immunoprecipitation assays, both Net1 and Tof2 lose binding to their rDNA sites in ulp2Δ cells and both factors largely regain this association in ulp2Δ slx5Δ A parsimonious interpretation of these results is that hypersumoylation of these proteins causes them to be ubiquitylated by Slx5/Slx8, impairing their association with rDNA. Fob1, a protein that anchors both Net1 and Tof2 to the replication-fork barrier (RFB) in the rDNA repeats, is sumoylated in wild-type...Continue Reading

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Citations

Jun 16, 2018·The Journal of Biological Chemistry·Claudio Ponte de AlbuquerqueHuilin Zhou
Sep 3, 2016·Genes & Development·Hong-Yeoul RyuMark Hochstrasser
Dec 24, 2018·Nature Communications·Hong-Yeoul RyuMark Hochstrasser
May 18, 2017·Genes & Development·Nalini Dhingra, Xiaolan Zhao
Aug 9, 2019·Current Genetics·Chihiro Horigome, Takehiko Kobayashi
Nov 25, 2020·Nucleic Acids Research·Hong-Yeoul RyuMark Hochstrasser
Feb 3, 2021·Molecular and Cellular Biology·D E MacNeilC Autexier

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