Yeast Uri1p promotes translation initiation and may provide a link to cotranslational quality control

Deplazes, Anna; Möckli, Natalie; Luke, Brian; Auerbach, Daniel; Peter, Matthias

doi:10.1038/emboj.2009.98

Cited by 37 publications

(58 citation statements)

References 39 publications

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“…The finding that specific residues of Rad52 cause a DSB repair defect without decreasing spontaneous HR (C180 mutated to A) [15] suggests that class C mutants of Rad52 preferentially affect SCE (Figure 1, Figure 2, Figure 3, and Figure S4). Importantly our study also describes a number of new genes with specific roles in SCR, which include factors of unknown function such as Irc4, Irc9 and Irc19, the SUMO/Ub-SUMO protease Wss1 [16], the Bud27 and Pdr10 proteins involved in stress response [19], [20], as well as proteins involved in chromatin remodeling, such as Ahc1 (structural subunit of the ADA histone acetyltransferase complex), Ada2 (Transcription coactivator, component of ADA and SAGA complexes [17], [21] and Rtt109 and Hst3, involved respectively in acetylation and deacetylation of histone H3 lysine 56 (H3K56), a core domain residue that localizes at both the entry and exit points of a nucleosome [6], [12], [22] …”

Section: Resultsmentioning

confidence: 99%

Histone H3K56 Acetylation, Rad52, and Non-DNA Repair Factors Control Double-Strand Break Repair Choice with the Sister Chromatid

et al. 2013

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DNA double-strand breaks (DSBs) are harmful lesions that arise mainly during replication. The choice of the sister chromatid as the preferential repair template is critical for genome integrity, but the mechanisms that guarantee this choice are unknown. Here we identify new genes with a specific role in assuring the sister chromatid as the preferred repair template. Physical analyses of sister chromatid recombination (SCR) in 28 selected mutants that increase Rad52 foci and inter-homolog recombination uncovered 8 new genes required for SCR. These include the SUMO/Ub-SUMO protease Wss1, the stress-response proteins Bud27 and Pdr10, the ADA histone acetyl-transferase complex proteins Ahc1 and Ada2, as well as the Hst3 and Hst4 histone deacetylase and the Rtt109 histone acetyl-transferase genes, whose target is histone H3 Lysine 56 (H3K56). Importantly, we use mutations in H3K56 residue to A, R, and Q to reveal that H3K56 acetylation/deacetylation is critical to promote SCR as the major repair mechanism for replication-born DSBs. The same phenotype is observed for a particular class of rad52 alleles, represented by rad52-C180A, with a DSB repair defect but a spontaneous hyper-recombination phenotype. We propose that specific Rad52 residues, as well as the histone H3 acetylation/deacetylation state of chromatin and other specific factors, play an important role in identifying the sister as the choice template for the repair of replication-born DSBs. Our work demonstrates the existence of specific functions to guarantee SCR as the main repair event for replication-born DSBs that can occur by two pathways, one Rad51-dependent and the other Pol32-dependent. A dysfunction can lead to genome instability as manifested by high levels of homolog recombination and DSB accumulation.

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Section: Resultsmentioning

confidence: 99%

Histone H3K56 Acetylation, Rad52, and Non-DNA Repair Factors Control Double-Strand Break Repair Choice with the Sister Chromatid

et al. 2013

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“…Indeed, BUD27 has also been shown to form a complex with the cotranslational quality control chaperones Ssb1p and Sis1p, as well as the elongation factor eEF1A, and to be somehow involved with initiating translation in yeast (Deplazes et al 2009). …”

Section: C19orf2 (Uri/rmp)mentioning

confidence: 99%

New insights into the biogenesis of nuclear RNA polymerases?This paper is one of a selection of papers published in this special issue entitled “Canadian Society of Biochemistry, Molecular & Cellular Biology 52nd Annual Meeting — Protein Folding: Principles and Diseases” and has undergone the Journal's usual peer review process.

Cloutier

Coulombe

2010

Biochem. Cell Biol.

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More than 30 years of research on nuclear RNA polymerases (RNAP I, II, and III) has uncovered numerous factors that regulate the activity of these enzymes during the transcription reaction. However, very little is known about the machinery that regulates the fate of RNAPs before or after transcription. In particular, the mechanisms of biogenesis of the 3 nuclear RNAPs, which comprise both common and specific subunits, remains mostly uncharacterized and the proteins involved are yet to be discovered. Using protein affinity purification coupled to mass spectrometry (AP-MS), we recently unraveled a high-density interaction network formed by nuclear RNAP subunits from the soluble fraction of human cell extracts. Validation of the dataset using a machine learning approach trained to minimize the rate of false positives and false negatives yielded a highconfidence dataset and uncovered novel interactors that regulate the RNAP II transcription machinery, including a set of proteins we named the RNAP II-associated proteins (RPAPs). One of the RPAPs, RPAP3, is part of an 11-subunit complex we termed the RPAP3/R2TP/prefoldin-like complex. Here, we review the literature on the subunits of this complex, which points to a role in nuclear RNAP biogenesis.

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“…URI was originally characterized in human and yeast cells as regulator of gene expression controlled by TOR (for target of Rapamycin) pathway [18]. Furthermore, URI has been linked to translation initiation [19], transcription regulation, chromatin stability or DNA damage response [13], [20]. URI is located mainly in the cytoplasm, although nuclear and perinuclear localization has also been observed in different organisms [20]–[22].…”

Section: Introductionmentioning

confidence: 99%

“…URI is located mainly in the cytoplasm, although nuclear and perinuclear localization has also been observed in different organisms [20]–[22]. However, in Saccharomyces cerevisiae , only a cytoplasmic localization has been detected [19]. In addition, URI is believed to function as a scaffold protein able to assemble additional members of PFD family (through its PFD- and Rpb5-binding domains) in both human and yeast [13], [23] and different authors have proposed a role in the cytoplasmic assembly of the human RNA pol II [8], [12], [13].…”

Section: Introductionmentioning

confidence: 99%

The Prefoldin Bud27 Mediates the Assembly of the Eukaryotic RNA Polymerases in an Rpb5-Dependent Manner

et al. 2013

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The unconventional prefoldin URI/RMP, in humans, and its orthologue in yeast, Bud27, have been proposed to participate in the biogenesis of the RNA polymerases. However, this role of Bud27 has not been confirmed and is poorly elucidated. Our data help clarify the mechanisms governing biogenesis of the three eukaryotic RNA pols. We show evidence that Bud27 is the first example of a protein that participates in the biogenesis of the three eukaryotic RNA polymerases and the first example of a protein modulating their assembly instead of their nuclear transport. In addition we demonstrate that the role of Bud27 in RNA pols biogenesis depends on Rpb5. In fact, lack of BUD27 affects growth and leads to a substantial accumulation of the three RNA polymerases in the cytoplasm, defects offset by the overexpression of RPB5. Supporting this, our data demonstrate that the lack of Bud27 affects the correct assembly of Rpb5 and Rpb6 to the three RNA polymerases, suggesting that this process occurs in the cytoplasm and is a required step prior to nuclear import. Also, our data support the view that Rpb5 and Rpb6 assemble somewhat later than the rest of the complexes. Furthermore, Bud27 Rpb5-binding but not PFD-binding domain is necessary for RNA polymerases biogenesis. In agreement, we also demonstrate genetic interactions between BUD27, RPB5, and RPB6. Bud27 shuttles between the nucleus and the cytoplasm in an Xpo1-independent manner, and also independently of microtubule polarization and possibly independently of its association with the RNA pols. Our data also suggest that the role of Bud27 in RNA pols biogenesis is independent of the chaperone prefoldin (PFD) complex and of Iwr1. Finally, the role of URI seems to be conserved in humans, suggesting conserved mechanisms in RNA pols biogenesis.

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Yeast Uri1p promotes translation initiation and may provide a link to cotranslational quality control

Cited by 37 publications

References 39 publications

Histone H3K56 Acetylation, Rad52, and Non-DNA Repair Factors Control Double-Strand Break Repair Choice with the Sister Chromatid

Histone H3K56 Acetylation, Rad52, and Non-DNA Repair Factors Control Double-Strand Break Repair Choice with the Sister Chromatid

The Prefoldin Bud27 Mediates the Assembly of the Eukaryotic RNA Polymerases in an Rpb5-Dependent Manner

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