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DNA clamp function of the monoubiquitinated Fanconi anaemia ID complex by Wang, Renjing; Wang, Shengliu; Dhar, Ankita; Peralta, Christopher; Pavletich, Nikola P. is a Physics and Astronomy article available to read on EtoBox.

What is DNA clamp function of the monoubiquitinated Fanconi anaemia ID complex about?

The ID complex, involving the proteins FANCI and FANCD2, is required for the repair of DNA interstrand crosslinks (ICL) and related lesions. These proteins are mutated in Fanconi anaemia, a disease in which patients are predisposed to cancer. The Fanconi anaemia pathway of ICL repair is activated when a replication fork stalls at an ICL; this triggers monoubiquitination of the ID complex, in which one ubiquitin molecule is conjugated to each of FANCI and FANCD2. Monoubiquitination of ID is essential for ICL repair by excision, translesion synthesis and homologous recombination; however, its function remains unknown. Here we report a cryo-electron microscopy structure of the monoubiquitinated human ID complex bound to DNA, and reveal that it forms a closed ring that encircles the DNA. By comparison with the structure of the non-ubiquitinated ID complex bound to ICL DNA-which we also report here-we show that monoubiquitination triggers a complete rearrangement of the open, trough-like ID structure through the ubiquitin of one protomer binding to the other protomer in a reciprocal fashion. These structures-together with biochemical data-indicate that the monoubiquitinated ID complex l

Who reads DNA clamp function of the monoubiquitinated Fanconi anaemia ID complex?

Author

Wang, Renjing; Wang, Shengliu; Dhar, Ankita; Peralta, Christopher; Pavletich, Nikola P.

Publisher

Nature Publishing Group; Springer Science and Business Media LLC; Society for Mining, Metallurgy and Exploration Inc.; Publons; ScienceOpen; Island Press (ISSN 0028-0836)

Published

2020

Language

EN

Field

Physics and Astronomy (Physical Sciences)