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 ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Cockayne Syndrome ◽  
Transcription Coupled Repair

scholarly journals The Cockayne syndrome group A gene encodes a WD repeat protein that interacts with CSB protein and a subunit of RNA polymerase II TFIIH

Cell ◽  
1995 ◽  
Vol 82 (4) ◽  
pp. 555-564 ◽  
Author(s):  
Karla A. Henning ◽  
Lei Li ◽  
Narayan Iyer ◽  
Lisa D. McDaniel ◽  
Michael S. Reagan ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Cockayne Syndrome ◽  
Repeat Protein ◽  
Group A ◽  
A Subunit ◽  
Wd Repeat

scholarly journals UV-induced proteolysis of RNA polymerase II is mediated by VCP/p97 segregase and timely orchestration by Cockayne syndrome B protein

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

scholarly journals Cockayne Syndrome A and B Proteins Differentially Regulate Recruitment of Chromatin Remodeling and Repair Factors to Stalled RNA Polymerase II In Vivo

2006 ◽  
Vol 23 (4) ◽  
pp. 471-482 ◽  
Author(s):  
Maria Fousteri ◽  
Wim Vermeulen ◽  
Albert A. van Zeeland ◽  
Leon H.F. Mullenders
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Chromatin Remodeling ◽  
Cockayne Syndrome

scholarly journals The Cockayne syndrome B protein, involved in transcription-coupled DNA repair, resides in an RNA polymerase II-containing complex

1997 ◽  
Vol 16 (19) ◽  
pp. 5955-5965 ◽  
Author(s):  
Alain J. van Gool ◽  
Elisabetta Citterio ◽  
Suzanne Rademakers ◽  
Roselinde van Os ◽  
Wim Vermeulen ◽  
...  
Keyword(s):  
Dna Repair ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Cockayne Syndrome

scholarly journals DNA damage stabilizes interaction of CSB with the transcription elongation machinery

2004 ◽  
Vol 166 (1) ◽  
pp. 27-36 ◽  
Author(s):  
Vincent van den Boom ◽  
Elisabetta Citterio ◽  
Deborah Hoogstraten ◽  
Angelika Zotter ◽  
Jean-Marc Egly ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Dna Damage ◽  
Dna Repair ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
High Molecular Weight ◽  
Transcription Elongation ◽  
Cockayne Syndrome ◽  
Dna Lesions ◽  
High Molecular Weight Complex

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.

scholarly journals Mechanism of Rad26-assisted rescue of stalled RNA polymerase II in transcription-coupled repair

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Chunli Yan ◽  
Thomas Dodd ◽  
Jina Yu ◽  
Bernice Leung ◽  
Jun Xu ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Bound States ◽  
Dna Lesions ◽  
Functional Interpretation ◽  
Structural Mechanism ◽  
Disease Mutations ◽  
Dynamic Communities ◽  
Allosteric Pathway ◽  
Transcription Coupled Repair

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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