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TAF2, within the TFIID complex, regulates the expression of a subset of protein-coding genes.
Cheng, I-Hsin; Pi, Wen-Chieh; Hsu, Chung-Hao; Guo, Yiran; Lai, Jun-Lin; Wang, Gang G; Chung, Bon-Chu; Roeder, Robert G; Chen, Wei-Yi.
Afiliación
  • Cheng IH; Institute of Biochemistry and Molecular Biology, National Yang Ming Chiao Tung University, Taipei, Taiwan.
  • Pi WC; Institute of Biochemistry and Molecular Biology, National Yang Ming Chiao Tung University, Taipei, Taiwan.
  • Hsu CH; School of Medicine, College of Medicine, National Yang Ming Chiao Tung University, Taipei, Taiwan.
  • Guo Y; Department of Pharmacology and Cancer Biology, Duke University School of Medicine, Durham, NC, 27710, USA.
  • Lai JL; Duke Cancer Institute, Durham, NC, 27710, USA.
  • Wang GG; Program in Molecular Medicine, National Yang Ming Chiao Tung University and Academia Sinica, Taipei, Taiwan.
  • Chung BC; Department of Pharmacology and Cancer Biology, Duke University School of Medicine, Durham, NC, 27710, USA.
  • Roeder RG; Duke Cancer Institute, Durham, NC, 27710, USA.
  • Chen WY; Insitute of Molecular Biology, Academia Sinica, Taipei, Taiwan.
Cell Death Discov ; 10(1): 244, 2024 May 21.
Article en En | MEDLINE | ID: mdl-38773077
ABSTRACT
TFIID, one of the general transcription factor (GTF), regulates transcriptional initiation of protein-coding genes through direct binding to promoter elements and subsequent recruitment of other GTFs and RNA polymerase II. Although generally required for most protein-coding genes, accumulated studies have also demonstrated promoter-specific functions for several TFIID subunits in gene activation. Here, we report that TBP-associated factor 2 (TAF2) specifically regulates TFIID binding to a small subset of protein-coding genes and is essential for cell growth of multiple cancer lines. Co-immunoprecipitation assays revealed that TAF2 may be sub-stoichiometrically associated with the TFIID complex, thus indicating a minor fraction of TAF2-containing TFIID in cells. Consistently, integrated genome-wide profiles show that TAF2 binds to and regulates only a small subset of protein-coding genes. Furthermore, through the use of an inducible TAF2 degradation system, our results reveal a reduction of TBP/TFIID binding to several ribosomal genes upon selective ablation of TAF2. In addition, depletion of TAF2, as well as the TAF2-regulated ribosomal protein genes RPL30 and RPL39, decreases ribosome assembly and global protein translation. Collectively, this study suggests that TAF2 within the TFIID complex is of functional importance for TBP/TFIID binding to and expression of a small subset of protein-coding genes, thus establishing a previously unappreciated promoter-selective function for TAF2.

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Idioma: En Revista: Cell Death Discov Año: 2024 Tipo del documento: Article País de afiliación: Taiwán

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Idioma: En Revista: Cell Death Discov Año: 2024 Tipo del documento: Article País de afiliación: Taiwán