TAF12 antibody - N-terminal region (P100965_P050)
- Known as:
- TAF12 (anti-) - N-terminal region (P100965_P050)
- Catalog number:
- p100965_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- TAF12 antibody - N-terminal region (P100965_P050)
Related genes to: TAF12 antibody - N-terminal region (P100965_P050)
- Gene:
- TAF12 NIH gene
- Name:
- TATA-box binding protein associated factor 12
- Previous symbol:
- TAF2J
- Synonyms:
- TAFII20
- Chromosome:
- 1p35.3
- Locus Type:
- gene with protein product
- Date approved:
- 1995-07-13
- Date modifiied:
- 2016-10-05
Related products to: TAF12 antibody - N-terminal region (P100965_P050)
Related articles to: TAF12 antibody - N-terminal region (P100965_P050)
- The fidelity of assembly of multiprotein complexes is essential for the formation of stable and functional protein complexes that are critical for cell growth and survival. In this context, TBP-associated factor (TAF) subunits maintain tight specificity for their integration into TFIID and SAGA complexes. In this work, using affinity purification-coupled mass spectrometry of epitope-tagged TFIID subunits TBP and TAF11, and the SAGA subunit TAF12L we identified components of the Candida albicans TFIID and SAGA complexes. Whereas TAF12 is a subunit of TFIID, the paralogous TAF12L is a subunit of the SAGA complex, and we further identified each of the TFIID and SAGA complex subunits with high confidence. We found that the steady-state levels of the histone fold domain containing pairs, TAF12-TAF4 and TAF12L-Ada1 proteins, are mutually dependent on the stable expression of each other. Using RNA immunoprecipitation from polysome-containing extracts, we found that nascent TAF4 and Ada1 proteins interact with TAF12 and TAF12L, respectively, by a cotranslational mechanism in an ordered, sequential mode of assembly. Our results further revealed that the intrinsic position of the histone fold domain within the protein sequence is crucial for determining the sequence and directionality of cotranslational assembly, ensuring both selectivity and stability of the histone fold domain containing heterodimeric proteins in the fungal pathogen C. albicans. - Source: PubMed
Publication date: 2026/02/04
Bhardwaj VidhiSwanson SeleneFlorens LaurenceWashburn Michael PWorkman Jerry LNatarajan Krishnamurthy - Metazoans utilize the small RNA pathway to regulate gene expression and maintain genome integrity. This pathway directs histone H3 lysine 9 tri-methylation (H3K9me3) or histone H3 lysine 27 tri-methylation (H3K27me3) at target loci to induce transcriptional gene silencing. Interestingly, some small RNAs are generated from genomic loci enriched in H3K9me3 or H3K27me3. However, the transcription mechanism of small RNA precursors from these heterochromatic regions remains unclear. In C. elegans, piRNAs originate from two genomic clusters enriched with H3K27me3 marks, which recruit the H3K27me3 reader UAD-2 and the upstream sequence transcription complex (USTC). Here, we demonstrate that piRNA transcription in C. elegans relies on TAF-12, a subunit of the basal transcription factor IID (TFIID). Depletion of TAF-12 reduces the production of both piRNA precursors and mature piRNAs. TAF-12 interacts with UAD-2 and facilitates piRNA focus formation in germ cell nuclei. We further show that TAF-12 triggers piRNA transcription by recruiting the RNA polymerase II subunit RPB-5, the Mediator complex subunit MDT-8, and the general transcription factors GTF-2F2 and GTF-2H2C. Thus, piRNA transcription within heterochromatic regions depends on the collaboration between histone modification readers, piRNA-specific transcription factors, and core transcription machinery. - Source: PubMed
Publication date: 2025/11/26
Huang XinyaKuang YanLi MeiliHong MinjieXu DeminCheng JieweiHuang TongtongSun XianleiWang WenkaiZhou YingFeng XuezhuChen XiangyangZhu ChengmingGuang Shouhong - The fidelity of assembly of multiprotein complexes is essential for the formation of stable and functional protein complexes that are critical for cell growth and survival. In this context, TBP-associated factor (TAF) subunits maintain tight specificity for their integration into TFIID and SAGA complexes. In this work, using affinity purification-coupled mass spectrometry of epitope-tagged TFIID subunits TBP and TAF11, and the SAGA subunit TAF12L we identified components of the TFIID and SAGA complexes. Whereas TAF12 is a subunit of TFIID, the paralogous TAF12L is a subunit of the SAGA complex, and we further identified each of the TFIID and SAGA complex subunits with high confidence. We found that the steady-state levels of the H2B-H2A-like histone fold domain containing pairs, TAF12-TAF4 and TAF12L-Ada1 proteins, are mutually dependent on the stable expression of each other. Using RNA coimmunoprecipitation from polysome-containing extracts, we found that nascent TAF4 and Ada1 proteins interact with TAF12 and TAF12L, respectively, by a cotranslational mechanism in an ordered, sequential mode of assembly. Thus, our results indicate that heterodimerization of the TAF12 paralogs with cognate partners occur by sequential cotranslational assembly thereby ensuring both selectivity and stability of the H2A-H2B heterodimers in fungal pathogen - Source: PubMed
Publication date: 2025/06/26
Bhardwaj VidhiSwanson SeleneFlorens LaurenceWashburn Michael PWorkman Jerry LNatarajan Krishnamurthy - Exosomes encompass a great deal of valuable biological information and play a critical role in tumor development. However, the mechanism of exosomal lncRNAs remains poorly elucidated in bladder cancer (BCa). In this study, we identified exosomal lnc-TAF12-2:1 as a novel biomarker in BCa diagnosis and aimed to investigate the underlying biological function. Dual luciferase reporter assay, RNA immunoprecipitation (RIP), RNA pulldown assays, and xenograft mouse model were used to verify the competitive endogenous RNA mechanism of lnc-TAF12-2:1. We found exosomal lnc-TAF12-2:1 up-regulated in urinary exosomes, tumor tissues of patients, and BCa cells. Down-regulation of lnc-TAF12-2:1 impaired BCa cell proliferation and migration, and promoted cell cycle arrest at the G0/G1 phase and cell apoptosis. The opposite effects were also observed when lnc-TAF12-2:1 was overexpressed. lnc-TAF12-2:1 was transferred by intercellular exosomes to modulate malignant biological behavior. Mechanistically, lnc-TAF12-2:1 packaged in the exosomes relieved the miRNA-mediated silence effect on ASB12 via serving as a sponger of miR-7847-3p to accelerate progression in BCa. ASB12 was also first proved as an oncogene to promote cell proliferation and migration and depress cell cycle arrest and cell apoptosis in our data. In conclusion, exosomal lnc-TAF12-2:1, located in the cytoplasm of BCa, might act as a competitive endogenous RNA to competitively bind to miR-7847-3p, and then be involved in miR-7847-3p/ASB12 regulatory axis to promote tumorigenesis, which provided a deeper insight into the molecular mechanism of BCa. - Source: PubMed
Publication date: 2024/08/05
Chen SongCheng JieLiu ShuangtaiShan DanniWang TingWang Xinghuan - Acute myeloid leukemia (AML) is characterized by several recurrent mutations that affect disease biology and phenotype, response to therapy and risk of subsequent relapse. Though tyrosine kinase inhibitors have gained regulatory approval for the treatment of AML, it is unclear whether single drugs targeting a specific genomic alteration will be sufficient to eradicate disease. Fortuitously, kinase/bromodomain inhibitors allow targeting of downstream transcriptional effectors of oncogenic pathways, allowing impediment of drug resistance at the transcriptional level. Successful development of combinatorial therapeutic strategies to inhibit both upstream oncogenic pathways and their downstream effectors could thus impede the onset of resistant disease. By using a combination of high-throughput cell-based screening assays and structure-based design, we have developed a novel anti-proliferative 3i-compound scaffold with a diverse range of single and dual FLT3/TAF1(2) activity against AML. Our novel approach to target both FLT3 kinase and TAF1(2) bromodomain efficiently maintained potency against haematological cancers. However, reference compounds and in vitro cell viability and cytotoxicity assays in cancer cell lines demonstrated superior effects of high affinity tyrosine kinase inhibition compared to inhibition of the TAF1 bromodomain. Our results highlight the feasibility of dual tyrosine kinase-bromodomain targeting to overcome disease mechanisms while also revealing the increased efficacy of FLT3-targeted compounds in AML. - Source: PubMed
Publication date: 2025/03/28
Leigh Robert SKaynak Bogac LRuskoaho HeikkiVälimäki Mika J