Rad23 links DNA repair to the ubiquitin/proteasome pathway

被引：400

作者：

Schauber, C ^{[1
]}

Chen, L ^{[1
]}

Tongaonkar, P ^{[1
]}

Vega, I ^{[1
]}

Lambertson, D ^{[1
]}

Potts, W ^{[1
]}

Madura, K ^{[1
]}

机构：

[1] Univ Med & Dent New Jersey, Robert Wood Johnson Med Sch, Dept Biochem, Piscataway, NJ 08854 USA

来源：

NATURE | 1998年 / 391卷 / 6668期

关键词：

D O I：

10.1038/35661

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Rad23 is an evolutionarily conserved protein that is important for nucleotide excision repair(1-3). A regulatory role has been proposed for Rad23 because rad23 mutants are sensitive to ultraviolet light but are still capable of incising damaged DNA(4,5). Here we show that Rad23 interacts with the 26S proteasome through an aminoterminal ubiquitin-like domain (UbL(R23)). The carboxy terminus of Rad23 binds to the Rad4 DNA repair protein and creates a link between the DNA repair and proteasome pathways. The ultraviolet sensitivity caused by deletion of the UbL(R23) domain may therefore arise from its inability to interact with the proteasome. The fusion proteins glutathione S-transferase (GST)-Rad23 and Rad4-haemagglutinin (HA), and the proteasome subunits Cim3 and Cim5, cofractionate through consecutive chromatography steps. The ubiquitin-like domain of human Rad23 (UbL(HRB)) also interacts with the human proteasome. These results demonstrate that ubiquitin-like domains (UbLs) represent a new class of proteasome-interacting motifs.

引用

页码：715 / 718

页数：4

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