Repair, Removal, and Shutdown: It All Hinges on RNA Polymerase II Ubiquitylation

Kook Son; Orlando D Schärer

doi:10.1016/j.cell.2020.02.053

Repair, Removal, and Shutdown: It All Hinges on RNA Polymerase II Ubiquitylation

Cell. 2020 Mar 19;180(6):1039-1041. doi: 10.1016/j.cell.2020.02.053.

Authors

Kook Son¹, Orlando D Schärer²

Affiliations

¹ Center for Genomic Integrity, Institute for Basic Science, Ulsan 44919, Republic of Korea.
² Center for Genomic Integrity, Institute for Basic Science, Ulsan 44919, Republic of Korea; School of Life Sciences, Ulsan National Institute of Science and Technology, Ulsan 44919, Republic of Korea. Electronic address: [email protected].

PMID: 32200798
DOI: 10.1016/j.cell.2020.02.053

Abstract

Two papers, by Nakazawa and Vidaković, show how ubiquitylation of a single lysine residue in RNA polymerase II serves as a master switch to regulate transcription, RNA polymerase II degradation, and transcription-coupled nucleotide excision repair in response to DNA damage.

Publication types

Comment

MeSH terms

DNA Damage
DNA Repair
RNA Polymerase II*
Transcription, Genetic*
Ubiquitination

Substances

RNA Polymerase II