TRiC controls transcription resumption after UV damage by regulating Cockayne syndrome protein A.
TRiC controls transcription resumption after UV damage by regulating Cockayne syndrome protein A.
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DOI：
10.1038/s41467-018-03484-6
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发表时间：
2018-03-12
影响因子：
16.6
通讯作者：
van Attikum H
中科院分区：
文献类型：
--
作者：
Pines A;Dijk M;Makowski M;Meulenbroek EM;Vrouwe MG;van der Weegen Y;Baltissen M;French PJ;van Royen ME;Luijsterburg MS;Mullenders LH;Vermeulen M;Vermeulen W;Pannu NS;van Attikum H
Transcription-blocking DNA lesions are removed by transcription-coupled nucleotide excision repair (TC-NER) to preserve cell viability. TC-NER is triggered by the stalling of RNA polymerase II at DNA lesions, leading to the recruitment of TC-NER-specific factors such as the CSA–DDB1–CUL4A–RBX1 cullin–RING ubiquitin ligase complex (CRLCSA). Despite its vital role in TC-NER, little is known about the regulation of the CRLCSA complex during TC-NER. Using conventional and cross-linking immunoprecipitations coupled to mass spectrometry, we uncover a stable interaction between CSA and the TRiC chaperonin. TRiC’s binding to CSA ensures its stability and DDB1-dependent assembly into the CRLCSA complex. Consequently, loss of TRiC leads to mislocalization and depletion of CSA, as well as impaired transcription recovery following UV damage, suggesting defects in TC-NER. Furthermore, Cockayne syndrome (CS)-causing mutations in CSA lead to increased TRiC binding and a failure to compose the CRLCSA complex. Thus, we uncover CSA as a TRiC substrate and reveal that TRiC regulates CSA-dependent TC-NER and the development of CS. An integrated network of chaperones and protein degradation machineries called the proteostasis network (PN) is required to maintain protein homeostasis. Here the authors show that one of the components of the PN, the chaperonin TRiC, interacts with the core transcription-coupled nucleotide excision repair protein CSA to ensure its assembly into the CRLCSA complex.
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影响因子：
14.8
作者：
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通讯作者：
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DOI：
10.1080/10253890701314863
发表时间：
2007-11-01
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