scholarly journals Rad26, the Yeast Homolog of the Cockayne Syndrome B Gene Product, Counteracts Inhibition of DNA Repair Due to RNA Polymerase II Transcription

1999 ◽  
Vol 274 (3) ◽  
pp. 1199-1202 ◽  
Author(s):  
Marcel Tijsterman ◽  
Jaap Brouwer
Keyword(s):  
Dna Repair ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Gene Product ◽  
Cockayne Syndrome ◽  
Yeast Homolog ◽  
Rna Polymerase Ii Transcription

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 Reduced RNA polymerase II transcription in intact and permeabilized Cockayne syndrome group B cells

1997 ◽  
Vol 94 (9) ◽  
pp. 4306-4311 ◽  
Author(s):  
A. S. Balajee ◽  
A. May ◽  
G. L. Dianov ◽  
E. C. Friedberg ◽  
V. A. Bohr
Keyword(s):  
B Cells ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Cockayne Syndrome ◽  
Group B ◽  
Rna Polymerase Ii Transcription

RAD25 is a DMA helicase required for DNA repair and RNA polymerase II transcription

Nature ◽  
1994 ◽  
Vol 369 (6481) ◽  
pp. 578-581 ◽  
Author(s):  
Sami N. Guzder ◽  
Patrick Sung ◽  
Véronique Bailly ◽  
Louise Prakash ◽  
Satya Prakash
Keyword(s):  
Dna Repair ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Rna Polymerase Ii Transcription

scholarly journals Evidence that the Transcription Elongation Function of Rpb9 Is Involved in Transcription-Coupled DNA Repair in Saccharomyces cerevisiae

2006 ◽  
Vol 26 (24) ◽  
pp. 9430-9441 ◽  
Author(s):  
Shisheng Li ◽  
Baojin Ding ◽  
Runqiang Chen ◽  
Christine Ruggiero ◽  
Xuefeng Chen
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Dna Repair ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Transcription Elongation ◽  
Elongation Factor ◽  
Complementation Group ◽  
Cockayne Syndrome ◽  
Transcription Repression ◽  
Group B

ABSTRACT Rpb9, a small nonessential subunit of RNA polymerase II, has been shown to have multiple transcription-related functions in Saccharomyces cerevisiae. These functions include promoting transcription elongation and mediating a subpathway of transcription-coupled repair (TCR) that is independent of Rad26, the homologue of human Cockayne syndrome complementation group B protein. Rpb9 is composed of three distinct domains: the N-terminal Zn1, the C-terminal Zn2, and the central linker. Here we show that the Zn1 and linker domains are essential, whereas the Zn2 domain is almost dispensable, for both transcription elongation and TCR functions. Impairment of transcription elongation, which does not dramatically compromise Rad26-mediated TCR, completely abolishes Rpb9-mediated TCR. Furthermore, Rpb9 appears to be dispensable for TCR if its transcription elongation function is compensated for by removing a transcription repression/elongation factor. Our data suggest that the transcription elongation function of Rpb9 is involved in TCR.

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