4.5 Article

Structural insights into assembly of transcription preinitiation complex

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CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2022.102404

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资金

  1. National Key R&D Program of China [2021YFA1300100]
  2. National Natural Science Foundation of China [32030055, 31830107, 31821002]
  3. Young Elite Scientists Sponsorship Program by CAST

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Researchers have made a breakthrough in determining the structure of TFIID-based PIC complexes, revealing the assembly mechanisms on TATA box and TATA-less promoters and providing a framework for further investigation of transcription initiation.
RNA polymerase II (Pol II)-mediated transcription in eukaryotic cells starts with assembly of preinitiation complex (PIC) on core promoter, a DNA sequence of similar to 100 base pairs. The transcription PIC consists of Pol II and general transcription factors TFIID, TFIIA, TFIIB, TFIIF, TFIIE, and TFIIH. Previous structural studies focused on PIC assembled on TATA box promoters with TFIID replaced by its subunit, TATA boxbinding protein (TBP). However, the megadalton TFIID complex is essential for promoter recognition, TBP loading onto promoter, and PIC assembly for almost all Pol II-mediated transcription, especially on the TATA-less promoters, which account for similar to 85% of core promoters of human coding genes. The functions of TFIID could not be replaced by TBP. The recent breakthrough in structure determination of TFIID-based PIC complexes in different assembly stages revealed mechanistic insights into PIC assembly on TATA box and TATA-less promotes and provided a framework for further investigation of transcription initiation.

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