Reference: Liu L, et al. (2019) Crystal structure of the yeast Rad7-Elc1 complex and assembly of the Rad7-Rad16-Elc1-Cul3 complex. DNA Repair (Amst) 77:1-9

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Abstract


Nucleotide excision repair (NER) is a versatile system that deals with various bulky and helix-distorting DNA lesions caused by UV and environmental mutagens. Based on how lesion recognition occurs, NER has been separated into global genome repair (GGR) and transcription-coupled repair (TCR). The yeast Rad7-Rad16 complex is indispensable for the GGR sub-pathway. Rad7-Rad16 binds to UV-damaged DNA in a synergistic fashion with RAD4, the main lesion recognizer, to achieve efficient recognition of lesions. In addition, Rad7-Rad16 associates with ELC1 and CUL3 to form an EloC-Cul-SOCS-box (ECS)-type E3 ubiquitin ligase complex that ubiquitinates RAD4 in response to UV radiation. However, the structure and architecture of the Rad7-Rad16-ELC1-CUL3 complex remain unsolved. Here, we determined the structure of the Rad7-ELC1 complex and revealed key interaction regions responsible for the formation of the Rad7-Rad16-ELC1-CUL3 complex. These results provide new insights into the assembly of the Rad7-Rad16-ELC1-CUL3 complex and structural framework for further studies.

Reference Type
Journal Article | Research Support, Non-U.S. Gov't
Authors
Liu L, Huo Y, Li J, Jiang T
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