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  Structural basis for RNA polymerase II ubiquitylation and inactivation in transcription-coupled repair

Kokic, G., Yakoub, G., van den Heuvel, D., Wondergem, A. P., van der Meer, P. J., van der Weegen, Y., et al. (2024). Structural basis for RNA polymerase II ubiquitylation and inactivation in transcription-coupled repair. Nature Structural & Molecular Biology, 31, 536-547. doi:10.1038/s41594-023-01207-0.

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Item Permalink: https://hdl.handle.net/21.11116/0000-000E-6403-E Version Permalink: https://hdl.handle.net/21.11116/0000-000F-2242-0
Genre: Journal Article

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 Creators:
Kokic, Goran1, Author           
Yakoub, George, Author
van den Heuvel, Diana, Author
Wondergem, Annelotte P., Author
van der Meer, Paula J., Author
van der Weegen, Yana, Author
Chernev, Aleksandar2, Author           
Fianu, Isaac1, Author           
Fokkens, Thornton J.3, Author           
Lorenz, Sonja3, Author                 
Urlaub, Henning2, Author           
Cramer, Patrick1, Author                 
Luijsterburg, Martijn S., Author
Affiliations:
1Department of Molecular Biology, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society, ou_3350224              
2Research Group of Bioanalytical Mass Spectrometry, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society, ou_3350290              
3Research Group Ubiquitin Signaling Specificity, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society, ou_3350289              

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 Abstract: During transcription-coupled DNA repair (TCR), RNA polymerase II (Pol II) transitions from a transcriptionally active state to an arrested state that allows for removal of DNA lesions. This transition requires site-specific ubiquitylation of Pol II by the CRL4CSA ubiquitin ligase, a process that is facilitated by ELOF1 in an unknown way. Using cryogenic electron microscopy, biochemical assays and cell biology approaches, we found that ELOF1 serves as an adaptor to stably position UVSSA and CRL4CSA on arrested Pol II, leading to ligase neddylation and activation of Pol II ubiquitylation. In the presence of ELOF1, a transcription factor IIS (TFIIS)-like element in UVSSA gets ordered and extends through the Pol II pore, thus preventing reactivation of Pol II by TFIIS. Our results provide the structural basis for Pol II ubiquitylation and inactivation in TCR.

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Language(s): eng - English
 Dates: 2024-02-052024-03
 Publication Status: Issued
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/s41594-023-01207-0
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Title: Nature Structural & Molecular Biology
  Other : Nature Structural and Molecular Biology
  Abbreviation : Nat Struct Mol Biol
Source Genre: Journal
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Publ. Info: New York, NY : Nature Pub. Group
Pages: - Volume / Issue: 31 Sequence Number: - Start / End Page: 536 - 547 Identifier: ISSN: 1545-9993
CoNE: https://pure.mpg.de/cone/journals/resource/954925603763