Sumoylation of the Yeast Gcn5 Protein

Sterner, David E.; Nathan, Dafna; Reindle, Alison; Johnson, Erica S.; Berger, Shelley L.

doi:10.1021/bi051624q

Cited by 28 publications

(23 citation statements)

References 40 publications

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“…Proteomics studies in the latter two organisms showed that the SAGA complex is also sumoylated at various subunits (Golebiowski et al, 2009; Makhnevych et al, 2009). In yeast, Gcn5 sumoylation appears to inhibit SAGA-mediated gene expression (Sterner et al, 2006), which agrees with the notion that sumoylation generally causes gene repression. In Arabidopsis, GCN5 is associated with about one third of 20,000 promoter regions analyzed (Benhamed et al, 2008).…”

Section: Sumoylation Of Conserved Subunits Of Chromatin-modifying Prosupporting

confidence: 59%

Global SUMO Proteome Responses Guide Gene Regulation, mRNA Biogenesis, and Plant Stress Responses

Mazur¹,

Burg²

2012

Front. Plant Sci.

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Small Ubiquitin-like MOdifier (SUMO) is a key regulator of abiotic stress, disease resistance, and development in plants. The identification of >350 plant SUMO targets has revealed many processes modulated by SUMO and potential consequences of SUMO on its targets. Importantly, highly related proteins are SUMO-modified in plants, yeast, and metazoans. Overlapping SUMO targets include heat-shock proteins (HSPs), transcription regulators, histones, histone-modifying enzymes, proteins involved in DNA damage repair, but also proteins involved in mRNA biogenesis and nucleo-cytoplasmic transport. Proteomics studies indicate key roles for SUMO in gene repression by controlling histone (de)acetylation activity at genomic loci. The responsible heavily sumoylated transcriptional repressor complexes are recruited by plant transcription factors (TFs) containing an (ERF)-associated Amphiphilic Repression (EAR) motif. These TFs are not necessarily themselves a SUMO target. Conversely, SUMO acetylation (Ac) prevents binding of downstream partners by blocking binding of their SUMO-interaction peptide motifs to Ac-SUMO. In addition, SUMO acetylation has emerged as a mechanism to recruit specifically bromodomains. Bromodomains are generally linked with gene activation. These findings strengthen the idea of a bi-directional sumo-acetylation switch in gene regulation. Quantitative proteomics has highlighted that global sumoylation provides a dynamic response to protein damage involving SUMO chain-mediated protein degradation, but also SUMO E3 ligase-dependent transcription of HSP genes. With these insights in SUMO function and novel technical advancements, we can now study SUMO dynamics in responses to (a)biotic stress in plants.

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Section: Sumoylation Of Conserved Subunits Of Chromatin-modifying Prosupporting

confidence: 59%

Global SUMO Proteome Responses Guide Gene Regulation, mRNA Biogenesis, and Plant Stress Responses

Mazur¹,

Burg²

2012

Front. Plant Sci.

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“…In cells, Siz1 has been reported to be present at only ~150 molecules/cell (Ghaemmaghami et al, 2003). This model might also account for the observation that often many subunits of a particular multisubunit complex are modified by SUMO (Denison et al, 2004;Hannich et al, 2005;Panse et al, 2004;Sterner et al, 2006;Wohlschlegel et al, 2004). Binding of a Siz protein to a complex might target multiple subunits for sumoylation simultaneously.…”

Section: Discussionmentioning

confidence: 98%

Multiple domains in Siz SUMO ligases contribute to substrate selectivity

Reindle

Belichenko

Bylebyl

et al. 2006

Journal of Cell Science

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124

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Saccharomyces cerevisiae contains two Siz/PIAS SUMO E3 ligases, Siz1 and Siz2/Nfi1, and one other known ligase, Mms21. Although ubiquitin ligases are highly substrate-specific, the degree to which SUMO ligases target distinct sets of substrates is unknown. Here we show that although Siz1 and Siz2 each have unique substrates in vivo, sumoylation of many substrates can be stimulated by either protein. Furthermore, in the absence of both Siz proteins, many of the same substrates are still sumoylated at low levels. Some of this residual sumoylation depends on MMS21. Siz1 targets its unique substrates through at least two distinct domains. Sumoylation of PCNA (proliferating cell nuclear antigen) and the splicing factor Prp45 requires part of the N-terminal region of Siz1, the `PINIT' domain, whereas sumoylation of the bud neck-associated septin proteins Cdc3, Cdc11 and Shs1/Sep7 requires the C-terminal domain of Siz1, which is also sufficient for cell cycle-dependent localization of Siz1 to the bud neck. Remarkably, the non-sumoylated septins Cdc10 and Cdc12 also undergo Siz1-dependent sumoylation if they are fused to the short ΨKXE SUMO attachment-site sequence. Collectively, these results suggest that local concentration of the E3, rather than a single direct interaction with the substrate polypeptide, is the major factor in substrate selectivity by Siz proteins.

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“…AllR mutant proteins, in which all lysines have mutated into arginines, have been used to reveal the functional relevance of SUMO modification in target proteins. Smt3 also has been successfully fused to the N-or C-terminus of target proteins to mimic constitutive sumoylation in vivo [55,56]. These fusion constructs lacked the C-terminal Gly-Gly residues of SUMO (i.e., the natural cleavage site), so that the SUMO structure formed but was not cleaved by endogenous SUMO proteases in yeast.…”

Section: Sumoylation Of Target Proteinsmentioning

confidence: 99%

Tying SUMO modifications to dynamic behaviors of chromosomes during meiotic prophase of Saccharomyces cerevisiae

Cheng

Lin

et al. 2007

J Biomed Sci

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In budding yeast Saccharomyces cerevisiae, centromeres and telomeres are tethered to the nuclear envelope during premeiotic interphase. Immediately after cells enter meiotic prophase, chromosomes undergo global reorganization, including bouquet formation (telomere clustering), non-homologous centromere coupling, homologous pairing, and assembly/disassembly of synaptonemal complexes. These chromosome dynamics have been implicated in promoting pairing, synapsis, crossover DNA recombination and segregation between homologous chromosomes. This review discusses recent studies related to the role of small ubiquitin-like modifier (SUMO) modification in controlling the overall budding yeast chromosome dynamics during meiotic prophase.

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Sumoylation of the Yeast Gcn5 Protein

Cited by 28 publications

References 40 publications

Global SUMO Proteome Responses Guide Gene Regulation, mRNA Biogenesis, and Plant Stress Responses

Global SUMO Proteome Responses Guide Gene Regulation, mRNA Biogenesis, and Plant Stress Responses

Multiple domains in Siz SUMO ligases contribute to substrate selectivity

Tying SUMO modifications to dynamic behaviors of chromosomes during meiotic prophase of Saccharomyces cerevisiae

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