scholarly journals Recognition of RNA Polymerase II and Transcription Bubbles by XPG, CSB, and TFIIH: Insights for Transcription-Coupled Repair and Cockayne Syndrome

2005 ◽  
Vol 20 (2) ◽  
pp. 187-198 ◽  
Author(s):  
Altaf H. Sarker ◽  
Susan E. Tsutakawa ◽  
Seth Kostek ◽  
Cliff Ng ◽  
David S. Shin ◽  
...  
Cell ◽  
1995 ◽  
Vol 82 (4) ◽  
pp. 555-564 ◽  
Author(s):  
Karla A. Henning ◽  
Lei Li ◽  
Narayan Iyer ◽  
Lisa D. McDaniel ◽  
Michael S. Reagan ◽  
...  

Oncotarget ◽  
2016 ◽  
Vol 8 (7) ◽  
pp. 11004-11019 ◽  
Author(s):  
Jinshan He ◽  
Qianzheng Zhu ◽  
Gulzar Wani ◽  
Altaf A. Wani

1997 ◽  
Vol 16 (19) ◽  
pp. 5955-5965 ◽  
Author(s):  
Alain J. van Gool ◽  
Elisabetta Citterio ◽  
Suzanne Rademakers ◽  
Roselinde van Os ◽  
Wim Vermeulen ◽  
...  

2004 ◽  
Vol 166 (1) ◽  
pp. 27-36 ◽  
Author(s):  
Vincent van den Boom ◽  
Elisabetta Citterio ◽  
Deborah Hoogstraten ◽  
Angelika Zotter ◽  
Jean-Marc Egly ◽  
...  

The Cockayne syndrome B (CSB) protein is essential for transcription-coupled DNA repair (TCR), which is dependent on RNA polymerase II elongation. TCR is required to quickly remove the cytotoxic transcription-blocking DNA lesions. Functional GFP-tagged CSB, expressed at physiological levels, was homogeneously dispersed throughout the nucleoplasm in addition to bright nuclear foci and nucleolar accumulation. Photobleaching studies showed that GFP-CSB, as part of a high molecular weight complex, transiently interacts with the transcription machinery. Upon (DNA damage-induced) transcription arrest CSB binding these interactions are prolonged, most likely reflecting actual engagement of CSB in TCR. These findings are consistent with a model in which CSB monitors progression of transcription by regularly probing elongation complexes and becomes more tightly associated to these complexes when TCR is active.


2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Chunli Yan ◽  
Thomas Dodd ◽  
Jina Yu ◽  
Bernice Leung ◽  
Jun Xu ◽  
...  

AbstractTranscription-coupled repair is essential for the removal of DNA lesions from the transcribed genome. The pathway is initiated by CSB protein binding to stalled RNA polymerase II. Mutations impairing CSB function cause severe genetic disease. Yet, the ATP-dependent mechanism by which CSB powers RNA polymerase to bypass certain lesions while triggering excision of others is incompletely understood. Here we build structural models of RNA polymerase II bound to the yeast CSB ortholog Rad26 in nucleotide-free and bound states. This enables simulations and graph-theoretical analyses to define partitioning of this complex into dynamic communities and delineate how its structural elements function together to remodel DNA. We identify an allosteric pathway coupling motions of the Rad26 ATPase modules to changes in RNA polymerase and DNA to unveil a structural mechanism for CSB-assisted progression past less bulky lesions. Our models allow functional interpretation of the effects of Cockayne syndrome disease mutations.


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