ArticleThe Journal of biological chemistry2011
Diverse roles of RNA polymerase II-associated factor 1 complex in different subpathways of nucleotide excision repair.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 34 citations in OpenAlex.
- PAF1c depletion confers chemoresistance to topoisomerase inhibitors.Cell insight · 2026Article
- Cdc73 protects Notch-induced T-cell leukemia cells from DNA damage and mitochondrial stress.Blood · 2023Article
- New roles for elongation factors in RNA polymerase II ubiquitylation and degradation.Biochimica et biophysica acta. Gene regulatory mechanisms · 2023Review
- Epigenetic Regulation of Nucleotide Excision Repair.Frontiers in cell and developmental biology · 2022Review
- The Paf1 Complex: A Keystone of Nuclear Regulation Operating at the Interface of Transcription and Chromatin.Journal of molecular biology · 2021Review
- Transcription-coupled nucleotide excision repair: New insights revealed by genomic approaches.DNA repair · 2021Review
- LEO1 is a partner for Cockayne syndrome protein B (CSB) in response to transcription-blocking DNA damage.Nucleic acids research · 2021Article
- Functional interplay between Mediator and RNA polymerase II in Rad2/XPG loading to the chromatin.Nucleic acids research · 2019Article
- Yeast PAF1 complex counters the pol III accumulation and replication stress on the tRNA genes.Scientific reports · 2019Article
- Histone H4 H75E mutation attenuates global genomic and Rad26-independent transcription-coupled nucleotide excision repair.Nucleic acids research · 2019Article
- Paf1 and Ctr9 subcomplex formation is essential for Paf1 complex assembly and functional regulation.Nature communications · 2018Article
- The Cellular Response to Transcription-Blocking DNA Damage.Trends in biochemical sciences · 2018Review
- Sen1, the yeast homolog of human senataxin, plays a more direct role than Rad26 in transcription coupled DNA repair.Nucleic acids research · 2016Article
- Ribosomopathies: Global process, tissue specific defects.Rare diseases (Austin, Tex.) · 2015Review
- Transcription bypass of DNA lesions enhances cell survival but attenuates transcription coupled DNA repair.Nucleic acids research · 2014Article
- Insights into how Spt5 functions in transcription elongation and repressing transcription coupled DNA repair.Nucleic acids research · 2014Article
- Cleavage factor I links transcription termination to DNA damage response and genome integrity maintenance in Saccharomyces cerevisiae.PLoS genetics · 2014Article
- The many roles of the conserved eukaryotic Paf1 complex in regulating transcription, histone modifications, and disease states.Biochimica et biophysica acta · 2013Article
- Implication of posttranslational histone modifications in nucleotide excision repair.International journal of molecular sciences · 2012Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transcription-coupled repair (TCR) and global genomic repair (GGR) are two pathways of nucleotide excision repair (NER). In Saccharomyces cerevisiae, Rad26 is important but not absolutely required for TCR. Rpb4, a nonessential RNA polymerase II (Pol II) subunit that forms a subcomplex with Rpb7, and the Spt4-Spt5 complex, a transcription elongation factor, have been shown to suppress Rad26-independent TCR. The Pol II-associated factor 1 complex (Paf1C) has been shown to function in transcription elongation, 3'-processing of mRNAs, and posttranslational modification of histones. Here we show that Paf1C plays a marginal role in facilitating Rad26-dependent TCR but significantly suppresses Rad26-independent TCR. The suppression of Rad26-independent TCR is achieved by cooperating with Spt4-Spt5. We propose a model that, in the absence of Rad26, a lesion is "locked" in the active center of a Pol II elongation complex, which is stabilized by the coordinated interactions of Rpb4-Rpb7, Spt4-Spt5, and Paf1C with each other and with the core Pol II. We also found that Paf1C facilitates GGR, especially in internucleosomal linker regions. The facilitation of GGR is achieved through enabling monoubiquitination of histone H2B lysine 123 by Bre1, which in turn permits di- and trimethylation of histone H3 lysine 79 by Dot1. To our best knowledge, among the NER-modulating factors documented so far, Paf1C appears to have the most diverse functions in different NER pathways or subpathways.
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