9B9L
RPRD1B C-terminal interacting domain bound to a pThr4 CTD peptide
Summary for 9B9L
| Entry DOI | 10.2210/pdb9b9l/pdb |
| Descriptor | 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) |
| Functional Keywords | complex, ctd, pol ii, thr4, transcription |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 3 |
| Total formula weight | 32089.24 |
| Authors | Moreno, R.Y.,Zhang, Y.J. (deposition date: 2024-04-02, release date: 2024-08-07, Last modification date: 2025-02-19) |
| Primary citation | 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 Cited by 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: 39241064DOI: 10.1126/sciadv.adq0350 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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