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Papers In Press, published online ahead of print December 8, 2003
Department of Biological Information, Tokyo Institute of Technology, Yokohama, Yokohama 226-8501
Corresponding Author: hhanda{at}bio.titech.ac.jp
DNA damage-induced ubiquitination of the RNA polymerase II largest subunit Rpb1 has been implicated in transcription-coupled repair for years. The studies so far, however, have been limited to the use of bulky, helix-distorting DNA damages caused by UV light and cisplatin, which are corrected by the nucleotide excision repair (NER) pathway. Non-bulky, non-helix-distorting damages are caused at high frequency by reactive oxygen species in cells and corrected by the base excision repair (BER) pathway. Contrary to a classic view, we recently found that the second type of DNA lesions also causes RNA polymerase II stalling in vitro. In this paper, we show that hydrogen peroxide (H2O2) causes significant ubiquitination and proteasomal degradation of Rpb1 by mechanisms that are distinct from those employed after UV irradiation. UV irradiation and H2O2 treatment cause characteristic changes in protein kinases phosphorylating its carboxy-terminal domain at Ser-2 and Ser-5. The H2O2-induced ubiquitination is likely dependent on unusual Ser-5 phosphorylation by ERK1/2. Moreover, the H2O2-induced ubiquitination occurs on transcriptionally engaged polymerases without a help of CSA, CSB, and pVHL proteins, which are all required for the UV-induced ubiquitination. These results suggest that stalled polymerases are recognized and ubiquitinated differentially depending on the types of DNA lesions. Our findings may have general implications in the basic mechanism of transcription-coupled NER and BER.
J. Biol. Chem, 10.1074/jbc.M311412200
Submitted on October 17, 2003
Revised on December 8, 2003
Accepted on December 8, 2003
A novel hydrogen peroxide-induced phosphorylation and ubiquitination pathway leading to RNA polymerase II proteolysis
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