6XRE

Structure of the p53/RNA polymerase II assembly

Summary for 6XRE

• Entry DOI: 10.2210/pdb6xre/pdb
• EMDB information: 22294
• Descriptor: DNA-directed RNA polymerase II subunit RPB1, DNA-directed RNA polymerases I, II, and III subunit RPABC5, DNA-directed RNA polymerase II subunit RPB11-a, ... (15 entities in total)
• Functional Keywords: activator, tumor suppressor, transcription, transferase
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 13
• Total formula weight: 561636.33

Authors

Liou, S.-H.,Singh, S.,Singer, R.H.,Coleman, R.A.,Liu, W. (deposition date: 2020-07-12, release date: 2021-03-24, Last modification date: 2024-03-06)

Primary citation

Liou, S.H.,Singh, S.K.,Singer, R.H.,Coleman, R.A.,Liu, W.L.
Structure of the p53/RNA polymerase II assembly.
Commun Biol, 4:397-397, 2021

PubMed Abstract: The tumor suppressor p53 protein activates expression of a vast gene network in response to stress stimuli for cellular integrity. The molecular mechanism underlying how p53 targets RNA polymerase II (Pol II) to regulate transcription remains unclear. To elucidate the p53/Pol II interaction, we have determined a 4.6 Å resolution structure of the human p53/Pol II assembly via single particle cryo-electron microscopy. Our structure reveals that p53's DNA binding domain targets the upstream DNA binding site within Pol II. This association introduces conformational changes of the Pol II clamp into a further-closed state. A cavity was identified between p53 and Pol II that could possibly host DNA. The transactivation domain of p53 binds the surface of Pol II's jaw that contacts downstream DNA. These findings suggest that p53's functional domains directly regulate DNA binding activity of Pol II to mediate transcription, thereby providing insights into p53-regulated gene expression.

PubMed: 33767390
DOI: 10.1038/s42003-021-01934-4

Experimental method

ELECTRON MICROSCOPY (4.6 Å)