9B9L

RPRD1B C-terminal interacting domain bound to a pThr4 CTD peptide

9B9L の概要

• エントリーDOI: 10.2210/pdb9b9l/pdb
• 分子名称: Regulation of nuclear pre-mRNA domain-containing protein 1B, SER-PRO-THR-SER-PRO-SER-TYR-SER-PRO-TPO-SER-PRO-SER-TYR-SER (3 entities in total)
• 機能のキーワード: complex, ctd, pol ii, thr4, transcription
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 32089.24

構造登録者

Moreno, R.Y.,Zhang, Y.J. (登録日: 2024-04-02, 公開日: 2024-08-07, 最終更新日: 2025-02-19)

主引用文献

Moreno, R.Y.,Panina, S.B.,Irani, S.,Hardtke, H.A.,Stephenson, R.,Floyd, B.M.,Marcotte, E.M.,Zhang, Q.,Zhang, Y.J.
Thr 4 phosphorylation on RNA Pol II occurs at early transcription regulating 3'-end processing.
Sci Adv, 10:eadq0350-eadq0350, 2024

PubMed Abstract: RNA polymerase II relies on a repetitive sequence domain (YSPTSPS) within its largest subunit to orchestrate transcription. While phosphorylation on serine-2/serine-5 of the carboxyl-terminal heptad repeats is well established, threonine-4's role remains enigmatic. Paradoxically, threonine-4 phosphorylation was only detected after transcription end sites despite functionally implicated in pausing, elongation, termination, and messenger RNA processing. Our investigation revealed that threonine-4 phosphorylation detection was obstructed by flanking serine-5 phosphorylation at the onset of transcription, which can be removed selectively. Subsequent proteomic analyses identified many proteins recruited to transcription via threonine-4 phosphorylation, which previously were attributed to serine-2. Loss of threonine-4 phosphorylation greatly reduces serine-2 phosphorylation, revealing a cross-talk between the two marks. Last, the function analysis of the threonine-4 phosphorylation highlighted its role in alternative 3'-end processing within pro-proliferative genes. Our findings unveil the true genomic location of this evolutionarily conserved phosphorylation mark and prompt a reassessment of functional assignments of the carboxyl-terminal domain.

PubMed: 39241064
DOI: 10.1126/sciadv.adq0350

実験手法

X-RAY DIFFRACTION (2.5 Å)