scholarly journals Diverse Roles of RNA Polymerase II-associated Factor 1 Complex in Different Subpathways of Nucleotide Excision Repair

2011 ◽  
Vol 286 (35) ◽  
pp. 30304-30313 ◽  
Author(s):  
Danielle Tatum ◽  
Wentao Li ◽  
Margaret Placer ◽  
Shisheng Li
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Nucleotide Excision Repair ◽  
Excision Repair ◽  
Associated Factor ◽  
Nucleotide Excision

Nucleotide excision repair in the yeast Saccharomyces cerevisiae : its relationship to specialized mitotic recombination and RNA polymerase II basal transcription

1995 ◽  
Vol 347 (1319) ◽  
pp. 63-68 ◽  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Nucleotide Excision Repair ◽  
Excision Repair ◽  
Gene Products ◽  
Basal Transcription ◽  
Yeast Saccharomyces Cerevisiae ◽  
Nucleotide Excision ◽  
Yeast Genes

Nucleotide excision repair (ner) in eukaryotes is a biochemically complex process involving multiple gene products. The budding yeast Saccharomyces cerevisiae is an informative model for this process. Multiple genes and in some cases gene products that are indispensable for ner have been isolated from this organism. Homologues of many of these yeast genes are structurally and functionally conserved in higher organisms, including humans. The yeast Rad1/Rad10 heterodimeric protein complex is an endonuclease that is believed to participate in damage-specific incision of DNA during ner . This endonuclease is also required for specialized types of recombination. The products of the RAD3, SSL2(RAD25) SSL1 and TFB1 genes have dual roles in ner and in RNA polymerase II-dependent basal transcription.

scholarly journals The yeast TFB1 and SSL1 genes, which encode subunits of transcription factor IIH, are required for nucleotide excision repair and RNA polymerase II transcription.

1995 ◽  
Vol 15 (4) ◽  
pp. 2288-2293 ◽  
Author(s):  
Z Wang ◽  
S Buratowski ◽  
J Q Svejstrup ◽  
W J Feaver ◽  
X Wu ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Nucleotide Excision Repair ◽  
Excision Repair ◽  
Temperature Sensitive ◽  
Restrictive Temperature ◽  
Yeast Saccharomyces Cerevisiae ◽  
Nucleotide Excision ◽  
Rna Polymerase Ii Transcription

The essential TFB1 and SSL1 genes of the yeast Saccharomyces cerevisiae encode two subunits of the RNA polymerase II transcription factor TFIIH (factor b). Here we show that extracts of temperature-sensitive mutants carrying mutations in both genes (tfb1-101 and ssl1-1) are defective in nucleotide excision repair (NER) and RNA polymerase II transcription but are proficient for base excision repair. RNA polymerase II-dependent transcription at the CYC1 promoter was normal at permissive temperatures but defective in extracts preincubated at a restrictive temperature. In contrast, defective NER was observed at temperatures that are permissive for growth. Additionally, both mutants manifested increased sensitivity to UV radiation at permissive temperatures. The extent of this sensitivity was not increased in a tfb1-101 strain and was only slightly increased in a ssl1-1 strain at temperatures that are semipermissive for growth. Purified factor TFIIH complemented defective NER in both tfb1-101 and ssl1-1 mutant extracts. These results define TFB1 and SSL1 as bona fide NER genes and indicate that, as is the case with the yeast Rad3 and Ss12 (Rad25) proteins, Tfb1 and Ssl1 are required for both RNA polymerase II basal transcription and NER. Our results also suggest that the repair and transcription functions of Tfb1 and Ssl1 are separable.

Yeast nucleotide excision repair proteins Rad2 and Rad4 interact with RNA polymerase II basal transcription factor b (TFIIH)

1994 ◽  
Vol 14 (6) ◽  
pp. 3569-3576
Author(s):  
A J Bardwell ◽  
L Bardwell ◽  
N Iyer ◽  
J Q Svejstrup ◽  
W J Feaver ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Nucleotide Excision Repair ◽  
Transcription Initiation ◽  
Excision Repair ◽  
Initiation Factor ◽  
Basal Transcription ◽  
Limited Region ◽  
Factor B ◽  
Nucleotide Excision

The Rad2, Rad3, Rad4, and Ss12 proteins are required for nucleotide excision repair in yeast cells and are homologs of four human proteins which are involved in a group of hereditary repair-defective diseases. We have previously shown that Rad3 protein is one of the five subunits of purified RNA polymerase II basal transcription initiation factor b (TFIIH) and that Ss12 protein physically associates with factor b (W.J. Feaver, J.Q. Svejstrup, L. Bardwell, A.J. Bardwell, S. Buratowski, K.D. Gulyas, T.F. Donahue, E.C. Friedberg, and R.D. Kornberg, Cell 75:1379-1387, 1993). Here we show that the Rad2 and Rad4 proteins interact with purified factor b in vitro. Rad2 (a single-stranded DNA endonuclease) specifically interacts with the Tfb1 subunit of factor b, and we have mapped a limited region of the Rad2 polypeptide which is sufficient for this interaction. Rad2 also interacts directly with Ss12 protein (a putative DNA helicase). The binding of Rad2 and Rad4 proteins to factor b may define intermediates in the assembly of the nucleotide excision repair repairosome. Furthermore, the loading of factor b (or such intermediates) onto promoters during transcription initiation provides a mechanism for the preferential targeting of repair proteins to actively transcribing genes.

scholarly journals Yeast RNA Polymerase II Transcription In Vitro Is Inhibited in the Presence of Nucleotide Excision Repair: Complementation of Inhibition by Holo-TFIIH and Requirement for RAD26

1998 ◽  
Vol 18 (5) ◽  
pp. 2668-2676 ◽  
Author(s):  
Zhaoyang You ◽  
William J. Feaver ◽  
Errol C. Friedberg
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Nucleotide Excision Repair ◽  
Excision Repair ◽  
Cell Extracts ◽  
Nucleotide Excision ◽  
Rnap Ii ◽  
Group B ◽  
Damaged Dna

ABSTRACT The Saccharomyces cerevisiae transcription factor IIH (TFIIH) is essential both for transcription by RNA polymerase II (RNAP II) and for nucleotide excision repair (NER) of damaged DNA. We have established cell extracts which support RNAP II transcription from the yeast CYC1 promoter or NER of transcriptionally silent damaged DNA on independent plasmid templates and substrates. When plasmid templates and substrates for both processes are simultaneously incubated with these extracts, transcription is significantly inhibited. This inhibition is strictly dependent on active NER and can be complemented with purified holo-TFIIH. These results suggest that in the presence of active NER, TFIIH is preferentially mobilized from the basal transcription machinery for use in NER. Inhibition of transcription in the presence of active NER requires theRAD26 gene, the yeast homolog of the human Cockayne syndrome group B gene (CSB).

scholarly journals Transcription-coupled nucleotide excision repair is coordinated by ubiquitin and SUMO in response to ultraviolet irradiation

2019 ◽  
Author(s):  
Frauke Liebelt ◽  
Joost Schimmel ◽  
Matty Verlaan – de Vries ◽  
Esra Klemann ◽  
Martin E van Royen ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Nucleotide Excision Repair ◽  
Uv Irradiation ◽  
Excision Repair ◽  
Premature Aging ◽  
Dependent Manner ◽  
Ubiquitin Ligase Complex ◽  
Nucleotide Excision ◽  
Damage Response

Abstract Cockayne Syndrome (CS) is a severe neurodegenerative and premature aging autosomal-recessive disease, caused by inherited defects in the CSA and CSB genes, leading to defects in transcription-coupled nucleotide excision repair (TC-NER) and consequently hypersensitivity to ultraviolet (UV) irradiation. TC-NER is initiated by lesion-stalled RNA polymerase II, which stabilizes the interaction with the SNF2/SWI2 ATPase CSB to facilitate recruitment of the CSA E3 Cullin ubiquitin ligase complex. However, the precise biochemical connections between CSA and CSB are unknown. The small ubiquitin-like modifier SUMO is important in the DNA damage response. We found that CSB, among an extensive set of other target proteins, is the most dynamically SUMOylated substrate in response to UV irradiation. Inhibiting SUMOylation reduced the accumulation of CSB at local sites of UV irradiation and reduced recovery of RNA synthesis. Interestingly, CSA is required for the efficient clearance of SUMOylated CSB. However, subsequent proteomic analysis of CSA-dependent ubiquitinated substrates revealed that CSA does not ubiquitinate CSB in a UV-dependent manner. Surprisingly, we found that CSA is required for the ubiquitination of the largest subunit of RNA polymerase II, RPB1. Combined, our results indicate that the CSA, CSB, RNA polymerase II triad is coordinated by ubiquitin and SUMO in response to UV irradiation. Furthermore, our work provides a resource of SUMO targets regulated in response to UV or ionizing radiation.

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