Hierarchical TAF1-dependent co-translational assembly of the basal transcription factor TFIID

Bernardini, Andrea; Mukherjee, Pooja; Scheer, Elisabeth; Kamenova, Ivanka; Antonova, Simona; Sanchez, Paulina Karen Mendoza; Yayli, Gizem; Morlet, Bastien; Timmers, Marc; Tora, Làszlò

doi:10.1038/s41594-023-01026-3

Cited by 13 publications

(17 citation statements)

References 62 publications

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“…3A). In line with similar observations for other complexes [115][116][117], this genetically encoded arrangement of interaction domains within primary sequences would thus impose an ordered assembly through co-translational events. In addition, the NPC co-translational interaction map shows a high representation of Nups harboring ID or SLiM domains (Box 1) [30].…”

Section: When Npc Assembly Begins During Translationsupporting

confidence: 80%

Puzzling out nuclear pore complex assembly

Penzo,

Palancade

2023

FEBS Letters

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Nuclear pore complexes (NPCs) are sophisticated multiprotein assemblies embedded within the nuclear envelope and controlling the exchanges of molecules between the cytoplasm and the nucleus. In this review, we summarize the mechanisms by which these elaborate complexes are built from their subunits, the nucleoporins, based on our ever‐growing knowledge of NPC structural organization and on the recent identification of additional features of this process. We present the constraints faced during the production of nucleoporins, their gathering into oligomeric complexes, and the formation of NPCs within nuclear envelopes, and review the cellular strategies at play, from co‐translational assembly to the enrolment of a panel of cofactors. Remarkably, the study of NPCs can inform our perception of the biogenesis of multiprotein complexes in general – and vice versa.

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Section: When Npc Assembly Begins During Translationsupporting

confidence: 80%

Puzzling out nuclear pore complex assembly

Penzo,

Palancade

2023

FEBS Letters

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“…To understand if TFIID can form biomolecular condensates in cells, we explored the nuclear distribution patterns of all individual TFIID subunits. To this end, we inducibly expressed each TFIID subunit fused to GFP under the control of a tet-inducible promoter in HeLa cells (Flp-In T-Rex system 12,13 ). Live-cell confocal high-resolution imaging revealed a range of different cellular distribution patterns of TBP and the TAFs (Figs.…”

Section: Taf2 Accumulates In Nuclear Speckles In Human Cellsmentioning

confidence: 99%

“…1A). Individual TAFs regulate different aspects of TFIID function, such as TFIID complex assembly (TAF1 12 ), TFIID complex integrity (TAF5/6/9 13 ), and promoter recognition (TAF1/2/4/7 10,11,14 ). Expectedly, TAFs are essential genes as gene deletions in mice are embryonically lethal [15][16][17] .…”

Section: Introductionmentioning

confidence: 99%

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TAF2 condensation in nuclear speckles links basal transcription factor TFIID to RNA splicing

Bhuiyan,

Mendoza Sanchez,

Arecco

et al. 2024

Preprint

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SummaryTFIID is an essential basal transcription factor, crucial for RNA polymerase II (pol II) promoter recognition and transcription initiation. The TFIID complex consists of the TATA-binding protein (TBP) and 13 TBP-associated factors (TAFs) that contain intrinsically disordered regions (IDRs) with currently unknown functions. Here, we show that a conserved IDR drives TAF2 condensation in nuclear speckles, independently of other TFIID subunits. Quantitative mass spectrometry analyses reveal that the TAF2 IDR specifically interacts with the nuclear speckle and spliceosome-associated protein SRRM2. Consequently, TAF2 recruits SRRM2 to TFIID to form non-canonical TFIID-SRRM2 complexes. Reduced SRRM2 recruitment elicits alternative splicing events in RNAs coding for proteins involved in transcription and transmembrane transport. Further, genome-wide binding analyses suggest TAF2 shuttling between nuclear speckles and pol II promoters. This study identifies an IDR of the basal transcription machinery as a molecular guide for protein partitioning into nuclear compartments, controlling protein complex composition and pre-mRNA splicing.

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“…In the latter, translation, folding, and assembly occur simultaneously, which can help funneling the assembly pathway of complexes, minimizing promiscuous interactions, or regulating orphan subunit degradation 21,22 . Recent reports have shown that co-translational assembly is prevalent [23][24][25][26][27] . In particular, Bertolini et al 28 identified thousands of proteins undergoing co-translational assembly by sequencing footprints protected among isolated disomes, i.e., pairs of ribosomes connected by their respective, interacting, nascent chains.…”

Section: Introductionmentioning

confidence: 99%

Structural determinants of co-translational protein complex assembly

Mallik,

Venezian,

Lobov

et al. 2024

Preprint

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The assembly of proteins into functional complexes is critical to life's processes. While textbooks depict complex assembly as occurring between fully synthesized proteins, we know today that thousands of proteins in the human proteome assemble co-translationally during their synthesis. Why this process takes place, however, remains unknown. We show that co-translational assembly is governed by biophysical and structural characteristics of the protein complex, and involves mutually stabilized, intertwined subunits. Consequently, these subunits are also co-regulated across the central dogma, from transcription to protein degradation. Leveraging structural signatures with AlphaFold2-based predictions enables us to accurately predict co-translational assembly on a proteome-wide scale, which we validated by ribosome profiling, genetic perturbations, and smFISH experiments. Notably, the latter showed that co-translationally assembling subunits exhibit co-localized mRNAs. This work unveils a fundamental connection between protein structure and the translation process, highlighting the overarching impact of three-dimensional structure on gene expression, mRNA localization, and proteostasis.

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Hierarchical TAF1-dependent co-translational assembly of the basal transcription factor TFIID

Cited by 13 publications

References 62 publications

Puzzling out nuclear pore complex assembly

Puzzling out nuclear pore complex assembly

TAF2 condensation in nuclear speckles links basal transcription factor TFIID to RNA splicing

Structural determinants of co-translational protein complex assembly

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