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Identification of interactions of Taf2 and Taf14 proteins.

ABSTRACT: Identification of proteins interacting with: 1. Full-length Taf14 2. Taf14-ET domain 3. Full-length Taf2 4. Taf2-deltaC

INSTRUMENT(S): LTQ Orbitrap XL

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Arnold Kristjuhan

LAB HEAD: Arnold Kristjuhan

PROVIDER: PXD032862 | Pride | 2022-10-13

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	190308_03_Orbi2_SK_SER_G90_T125_TYTI_Ilves_neg_cntrl_152.raw	Raw
	190308_05_Orbi2_SK_SER_G90_T125_TYTI_Ilves_Taf2-dC_1900.raw	Raw
	190308_07_Orbi2_SK_SER_G90_T125_TYTI_Ilves_Taf2_wt_2062.raw	Raw
	190620_07_Orbi2_KN_SER_G90_T125_TYTI_Ilves_2_1.raw	Raw
	190620_09_Orbi2_KN_SER_G90_T125_TYTI_Ilves_1_2.raw	Raw

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1 - 5 of 24

Publications

Transcriptional regulator Taf14 binds DNA and is required for the function of transcription factor TFIID in the absence of histone H2A.Z.

Peil Kadri K Värv Signe S Ilves Ivar I Kristjuhan Kersti K Jürgens Henel H Kristjuhan Arnold A

The Journal of biological chemistry 20220813 9

The transcriptional regulator Taf14 is a component of multiple protein complexes involved in transcription initiation and chromatin remodeling in yeast cells. Although Taf14 is not required for cell viability, it becomes essential in conditions where the formation of the transcription preinitiation complex is hampered. The specific role of Taf14 in mediating transcription initiation and preinitiation complex formation is unclear. Here, we explored its role in the general transcription factor IID ...[more]

PMID: 35970389

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Project description:TAF2 is the second largest subunit of general transcription factor TFIID. Although TFIID complex is putatively considered as a general initiation factor, gene-specific functions have been reported for several TAF subunits within it. To gain insights for TAF2 function in transcriptional regulation, genomic occupancy of TAF2 and transcriptiome of cells depleted of TAF2 are examined.

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TAF2 condensation in nuclear speckles links basal transcription factor TFIID to RNA splicing [CUT&RUN]

Project description:TFIID 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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Taf2 mediates DNA binding of Taf14

Project description:The assembly and function of the yeast general transcription factor TFIID complex requires specific contacts between its Taf14 and Taf2 subunits, however, the mechanism underlying these contacts remains unclear. Here, we determined the molecular and structural basis by which the YEATS and ET domains of Taf14 bind to the C-terminal tail of Taf2 and identified a unique DNA-binding activity of the linker region connecting the two domains. We show that in the absence of ligands the linker region of Taf14 is occluded by the surrounding domains, and therefore the DNA binding function of Taf14 is autoinhibited. Binding of Taf2 promotes a conformational rearrangement in Taf14, resulting in a release of the linker for the engagement with DNA and the nucleosome. Genetic in vivo data indicate that the association of Taf14 with both Taf2 and DNA is essential for transcriptional regulation. Our findings provide a basis for deciphering the role of individual TFIID subunits in mediating gene transcription.

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Cytoplasmic complex comprising TAF2, TAF8, TAF10 provides evidence for nuclear holo-TFIID assembly from preformed submodules

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2008-06-11 | E-GEOD-10021 | biostudies-arrayexpress

Importance of TAF8 regions for TFIID lobe B assembly, or for TAF2 interactions, are required for embryonic stem cell survival

Project description:The human general transcription factor TFIID is composed of the TATA-binding protein (TBP) and 13 TBP-associated factors (TAFs). In eukaryotic cells, TFIID is thought to nucleate RNA polymerase II (Pol II) preinitiation complex formation on all protein coding gene promoters and thus, be crucial for Pol II transcription. TFIID is composed of three lobes, named A, B and C. Structural studies showed that TAF8 is forming a histone fold pair in lobe B and connecting lobe B to lobe C. In the present study, we have investigated the requirement of the different regions of TAF8 for in vitro TFIID assembly, and the importance of certain TAF8 regions for mouse embryonic stem cell (ESC) viability. We have identified a TAF8 region, different from the histone fold domain of TAF8, important for assembling with the 5TAF core complex in lobe B, and four regions of TAF8 each individually required for interacting with TAF2 in lobe C. Moreover, we show that the 5TAF core-interacting TAF8 domain, and the proline rich domain of TAF8 interacting with TAF2, are both required for mouse embryonic stem cell survival. Thus, our study demonstrates that TAF8 regions involving in the connection of lobe B to lobe C are crucial for TFIID function and consequent ESC survival.

2022-02-15 | PXD028352 | Pride

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

Project description:TFIID is an essential eukaryotic transcription factor, which is required for RNA polymerase II promoter recognition and activation. As a multiprotein complex, TFIID contains several intrinsically disordered regions (IDRs), but the functions of these IDRs are unknown. Here, we show that a conserved IDR drives the TFIID subunit TAF2 to nuclear speckles, where it forms biomolecular condensates, separate from the TFIID complex. Quantitative mass spectrometry analyses reveal that the TAF2 IDR is required for the interaction with the nuclear speckle and spliceosome-associated protein SRRM2, which is thereby recruited to TFIID. The formation of SRRM2-free TFIID complexes elicits a set of unique alternative splicing events. These include events in RNAs coding for proteins involved in transcription and transmembrane transport. Together, these data identify an IDR of the basal transcription machinery as a molecular switch between nuclear compartments to control protein complex composition and pre-mRNA splicing.

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