The Rts1 Regulatory Subunit of PP2A Phosphatase Controls Expression of the HO Endonuclease via Localization of the Ace2 Transcription Factor

Parnell, Emily J.; Yu, Yan; Lucena, Rafael; Yoon, Yonghan; Bai, Lu; Kellogg, Douglas R.; Stillman, David J.

doi:10.1074/jbc.m114.611715

Cited by 9 publications

(6 citation statements)

References 22 publications

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“…The SBF transcription factor complex also promotes histone gene expression in late G1 (Eriksson et al 2012). Therefore, a mechanism may involve PP2A Rts1 promoting cell-cycle-regulated transcription through SBF or other G1 activators as reported previously for the G1 cyclin Cln3 (Artiles et al 2009;Parnell et al 2014;Zapata et al 2014) or negative regulation of a repressor similar to that reported for Ash1 . Indeed, Swi4, the DNA-binding subunit of SBF, was found to be hyperphosphorylated in rts1D cells (Zapata et al 2014).…”

Section: Discussionmentioning

confidence: 81%

“…We were intrigued by the third possibility, as RTS1 had previously been found to promote cell-cycle-regulated gene expression (Artiles et al 2009;Parnell et al 2014;Zapata et al 2014) and RTS1 overexpression suppressed gcn5D's slow G1-S progression ( Figure 2D). To test a role in histone expression, we quantified unmodified H3 levels along with the other core histones in WT and gcn5D by immunoblotting and found that gcn5D cells had reduced levels of core histones compared to WT ( Figure S4, A and B).…”

Section: Rts1 Overexpression Restores Histone Gene Expression In Gcn5mentioning

confidence: 99%

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Promotion of Cell Viability and Histone Gene Expression by the Acetyltransferase Gcn5 and the Protein Phosphatase PP2A in Saccharomyces cerevisiae

et al. 2016

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Histone modifications direct chromatin-templated events in the genome and regulate access to DNA sequence information. There are multiple types of modifications, and a common feature is their dynamic nature. An essential step for understanding their regulation, therefore, lies in characterizing the enzymes responsible for adding and removing histone modifications. Starting with a dosagesuppressor screen in Saccharomyces cerevisiae, we have discovered a functional interaction between the acetyltransferase Gcn5 and the protein phosphatase 2A (PP2A) complex, two factors that regulate post-translational modifications. We find that RTS1, one of two genes encoding PP2A regulatory subunits, is a robust and specific high-copy suppressor of temperature sensitivity of gcn5D and a subset of other gcn5D phenotypes. Conversely, loss of both PP2A Rts1 and Gcn5 function in the SAGA and SLIK/SALSA complexes is lethal. RTS1 does not restore global transcriptional defects in gcn5D; however, histone gene expression is restored, suggesting that the mechanism of RTS1 rescue includes restoration of specific cell cycle transcripts. Pointing to new mechanisms of acetylation-phosphorylation cross-talk, RTS1 high-copy rescue of gcn5D growth requires two residues of H2B that are phosphorylated in human cells. These data highlight the potential significance of dynamic phosphorylation and dephosphorylation of these deeply conserved histone residues for cell viability. KEYWORDS chromatin; transcription; phosphorylation; acetylation (IOC2, PAB1, RHO2, MED6, ZDS1, PP2A B56 ) A T the foundation of nuclear DNA organization in eukaryotes is the dynamic formation, movement, and modification of nucleosomes. Acetylation and phosphorylation are two histone post-translational modifications (PTMs) catalyzed by histone acetyltransferases (HATs) and kinases and reversed by histone deacetylases (HDACs) and phosphatases that alter nucleosome structure and function. Tightly regulated acetylation and phosphorylation of specific histone residues have deeply conserved functions in eukaryotes that are critical for transcriptional regulation, replication, repair, and segregation of eukaryotic genomes (Banerjee and Chakravarti 2011;Rossetto et al. 2012;Tessarz and Kouzarides 2014).One well-conserved HAT is Gcn5, which specifically targets histones H3 and H2B as part of multiple complexes (Grant et al. 1997;Eberharter et al. 1999;Grant et al. 1999;Howe et al. 2001;Sterner et al. 2002;Pray-Grant et al. 2005). Gcn5 is a key regulator of eukaryotic gene expression and acetylates H3 at promoters of active genes (Pokholok et al. 2005;Nagy and Tora 2007;Rosaleny et al. 2007). Its role as a transcriptional activator is so fundamental that Gcn5 is essential in most eukaryotes studied. An exception of note is budding yeast, where deletion of GCN5 is tolerated, but does cause a spectrum of phenotypes, including defects in gene activation, particularly for stress-regulated genes, and altered cell cycle progression (Howe et al. 2001;Huisinga and Pugh 2004;Vernarecci ...

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Section: Discussionmentioning

confidence: 81%

Section: Rts1 Overexpression Restores Histone Gene Expression In Gcn5mentioning

confidence: 99%

Promotion of Cell Viability and Histone Gene Expression by the Acetyltransferase Gcn5 and the Protein Phosphatase PP2A in Saccharomyces cerevisiae

et al. 2016

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“…Rts1 is important for the proper phosphorylation and localization of Ace2, a transcription factor required for expression in late mitosis and early G1 of genes involved in transport, ribosome biosynthesis, cell polarity, and septum destruction after cytokinesis, among other multiple functions [171]. Lack of Rts1 results in higher than normal presence of Ace2 in the mother cell nucleus, where it can activate ASH1, an inhibitor of the transcription of the HO endonuclease, leading to the blockage of HO expression in mother cells [172].…”

Section: Pp2a and Pp2a-like Phosphatasesmentioning

confidence: 99%

Ser/Thr protein phosphatases in fungi: structure, regulation and function

2019

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Reversible phospho-dephosphorylation of proteins is a major mechanism for the control of cellular functions. By large, Ser and Thr are the most frequently residues phosphorylated in eukar-yotes. Removal of phosphate from these amino acids is catalyzed by a large family of well-conserved enzymes, collectively called Ser/Thr protein phosphatases. The activity of these enzymes has an enormous impact on cellular functioning. In this work we pre-sent the members of this family in S. cerevisiae and other fungal species, and review the most recent findings concerning their regu-lation and the roles they play in the most diverse aspects of cell biology.

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“…In addition, PP2A Rts1 regulates the cell cycle entry into the next G1 by inhibiting the transcription factor Ace2 [27,106]. Rts1 is required for proper phosphorylation and localization of Ace2.…”

Section: The Role Of Pp2a In Cytokinesismentioning

confidence: 99%

PP2A Functions during Mitosis and Cytokinesis in Yeasts

Moyano-Rodríguez

Queralt

2019

IJMS

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Protein phosphorylation is a common mechanism for the regulation of cell cycle progression. The opposing functions of cell cycle kinases and phosphatases are crucial for accurate chromosome segregation and exit from mitosis. Protein phosphatases 2A are heterotrimeric complexes that play essential roles in cell growth, proliferation, and regulation of the cell cycle. Here, we review the function of the protein phosphatase 2A family as the counteracting force for the mitotic kinases. We focus on recent findings in the regulation of mitotic exit and cytokinesis by PP2A phosphatases in S. cerevisiae and other fungal species.

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The Rts1 Regulatory Subunit of PP2A Phosphatase Controls Expression of the HO Endonuclease via Localization of the Ace2 Transcription Factor

Cited by 9 publications

References 22 publications

Promotion of Cell Viability and Histone Gene Expression by the Acetyltransferase Gcn5 and the Protein Phosphatase PP2A in Saccharomyces cerevisiae

Promotion of Cell Viability and Histone Gene Expression by the Acetyltransferase Gcn5 and the Protein Phosphatase PP2A in Saccharomyces cerevisiae

Ser/Thr protein phosphatases in fungi: structure, regulation and function

PP2A Functions during Mitosis and Cytokinesis in Yeasts

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