Not5-dependent co-translational assembly of Ada2 and Spt20 is essential for functional integrity of SAGA

Kassem, Sari; Villányi, Zoltán; Collart, Martine A.

doi:10.1093/nar/gkw1059

Cited by 36 publications

(44 citation statements)

References 51 publications

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“…Recent work revealed widespread cotranslational assembly of protein complexes (Shiber et al, 2018), including S. cerevisiae SAGA (Kassem et al, 2017). In marked contrast, we did not observe evidence for cotranslational assembly of Tra1 and Tra2 into SAGA and NuA4, respectively.…”

Section: Cotranslation Interaction Between the Ttt Cochaperone And Itcontrasting

confidence: 99%

“…Cotranslational assembly has emerged as a prominent regulatory mechanism for promoting protein-protein interactions and the building of a complex (Duncan and Mata, 2011;Shiber et al, 2018;Shieh et al, 2015). Specifically, cotranslational interactions were observed for the SET1C histone methyltransferase complex (Halbach et al, 2009) and, more recently, between specific SAGA subunits (Kamenova et al, 2018;Kassem et al, 2017). Finally, a recent study demonstrated that Taf5, which is shared between SAGA and the general transcription factor TFIID, require a dedicated chaperone, the CCT chaperonin, for incorporation into pre-assembly modules (Antonova et al, 2018).…”

Section: Chaperone-mediated Cotranslational Folding Of Tra1 and Tra2 mentioning

confidence: 99%

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Chaperone-mediated ordered assembly of the SAGA and NuA4 transcription co-activator complexes

Elías-Villalobos

Toullec

Faux

et al. 2019

Preprint

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Transcription initiation involves the coordinated activities of large multimeric complexes.Little is known about the mechanisms and pathways that drive their assembly from individual components. We report here several principles underlying the assembly of the highly conserved SAGA co-activator complex, which is composed of 19 subunits organized into functional modules. First, we demonstrate that SAGA assembles through an ordered pathway, in which the core subunit Spt20 recruits Tra1, which then promotes the incorporation of the de-ubiquitination module (DUB). Second, affinity purifications and phenotypic analyses identified a small region of Spt20 that is both necessary and sufficient to anchor Tra1 to SAGA. Third, Tra1 is shared with the NuA4 co-activator complex and is the only pseudokinase of the PIKK family. We accumulated functional and biochemical evidence that Tra1 shares a specific Hsp90 cochaperone with PIKKs, the Triple-T complex, for its cotranslational folding and de novo incorporation into both SAGA and NuA4. Finally, in contrast to its specific role in SAGA assembly, Tra1 contributes to scaffold the entire NuA4 complex. Overall, our study brings mechanistic insights into the de novo assembly of transcriptional complexes via ordered pathways and reveals the contribution of dedicated chaperones to this process.

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Section: Cotranslation Interaction Between the Ttt Cochaperone And Itcontrasting

confidence: 99%

Section: Chaperone-mediated Cotranslational Folding Of Tra1 and Tra2 mentioning

confidence: 99%

Chaperone-mediated ordered assembly of the SAGA and NuA4 transcription co-activator complexes

Elías-Villalobos

Toullec

Faux

et al. 2019

Preprint

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“…Cotranslational association is favored in those cases where subunits are especially aggregation-prone [26]. Also yeast protein complexes, such as histone-modifying complexes methyl-transferase (SET1C) [115] and acetyltransferase (SAGA) assemble cotranslationally [116], as do cyclin protein complexes [117]. The ribosome may modulate the assembly of protein complexes by stabilizing individual protein domains or subunits [100] or adjusting the speed of translation [47] downstream of interaction domain boundaries [30].…”

Section: Cotranslational Subunits Assemblymentioning

confidence: 99%

Cotranslational Folding of Proteins on the Ribosome

2020

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Many proteins in the cell fold cotranslationally within the restricted space of the polypeptide exit tunnel or at the surface of the ribosome. A growing body of evidence suggests that the ribosome can alter the folding trajectory in many different ways. In this review, we summarize the recent examples of how translation affects folding of single-domain, multiple-domain and oligomeric proteins. The vectorial nature of translation, the spatial constraints of the exit tunnel, and the electrostatic properties of the ribosome-nascent peptide complex define the onset of early folding events. The ribosome can facilitate protein compaction, induce the formation of intermediates that are not observed in solution, or delay the onset of folding. Examples of single-domain proteins suggest that early compaction events can define the folding pathway for some types of domain structures. Folding of multi-domain proteins proceeds in a domain-wise fashion, with each domain having its role in stabilizing or destabilizing neighboring domains. Finally, the assembly of protein complexes can also begin cotranslationally. In all these cases, the ribosome helps the nascent protein to attain a native fold and avoid the kinetic traps of misfolding.

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“…Transporting a single mRNA is energetically efficient because a single mRNA molecule can be used to synthesize multiple copies of proteins, 43 reviewed more extensively here 2, 18, 44 . Similarly, colocalization of mRNAs encoding members of a protein complex could produce high concentrations of multisubunit complex components in a specific location, thus increasing complex formation efficiency and decreasing the formation of off‐target, nonfunctional complexes 45–48 . mRNAs can also be localized in a translationally silenced form.…”

Section: How Does Rna Get There?mentioning

confidence: 99%

“…Localization of these seven separate transcripts to protrusions aid in Arp2/3 assembly through local translation and assembly. In some cases, local translation of protein complex members can result in cotranslational assembly as observed for heteromeric ion channels 47 and histone acetyltransferase 48 …”

Section: How Does Rna Get There?mentioning

confidence: 99%

Mechanisms and consequences of subcellularRNAlocalization across diverse cell types

Engel

Arora

Goering

et al. 2020

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Essentially all cells contain a variety of spatially restricted regions that are important for carrying out specialized functions. Often, these regions contain specialized transcriptomes that facilitate these functions by providing transcripts for localized translation. These transcripts play a functional role in maintaining cell physiology by enabling a quick response to changes in the cellular environment. Here, we review how RNA molecules are trafficked within cells, with a focus on the subcellular locations to which they are trafficked, mechanisms that regulate their transport and clinical disorders associated with misregulation of the process. K E Y W O R D SRNA binding protein, RNA cis-element, RNA localization, RNA transport, zipcode

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Not5-dependent co-translational assembly of Ada2 and Spt20 is essential for functional integrity of SAGA

Cited by 36 publications

References 51 publications

Chaperone-mediated ordered assembly of the SAGA and NuA4 transcription co-activator complexes

Chaperone-mediated ordered assembly of the SAGA and NuA4 transcription co-activator complexes

Cotranslational Folding of Proteins on the Ribosome

Mechanisms and consequences of subcellularRNAlocalization across diverse cell types

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