RAD26/YJR035W Summary Help

Standard Name RAD26 1
Systematic Name YJR035W
Feature Type ORF, Verified
Description Protein involved in transcription-coupled nucleotide excision repair; repairs UV-induced DNA lesions; recruitment to DNA lesions is dependent on an elongating RNA polymerase II; homolog of human CSB protein (2, 3 and see Summary Paragraph)
Name Description RADiation sensitive
Chromosomal Location
ChrX:497355 to 500612 | ORF Map | GBrowse
Gbrowse
Gene Ontology Annotations All RAD26 GO evidence and references
  View Computational GO annotations for RAD26
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
High-throughput
Regulators 1 genes
Resources
Classical genetics
null
overexpression
Large-scale survey
null
overexpression
Resources
137 total interaction(s) for 110 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 22
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 1
  • Co-purification: 1
  • Two-hybrid: 14

Genetic Interactions
  • Dosage Growth Defect: 2
  • Dosage Lethality: 2
  • Dosage Rescue: 1
  • Negative Genetic: 20
  • Phenotypic Enhancement: 30
  • Phenotypic Suppression: 4
  • Positive Genetic: 9
  • Synthetic Growth Defect: 20
  • Synthetic Lethality: 1
  • Synthetic Rescue: 9

Resources
Expression Summary
histogram
Resources
Length (a.a.) 1,085
Molecular Weight (Da) 124,527
Isoelectric Point (pI) 7.47
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrX:497355 to 500612 | ORF Map | GBrowse
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..3258 497355..500612 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000003796
SUMMARY PARAGRAPH for RAD26

RAD26 encodes a DNA-dependent ATPase that plays a role in transcription-coupled repair (TCR) (4, 1). Rad26p mediates one of two subpathways of TCR; the second is mediated by Rpb9p, a nonessential subunit of RNA polymerase II (5). The relative contribution of each pathway may depend on the location of the damage relative to a gene (within the coding region vs. near the transcription start site) and its level of transcription (6, 7, 5, 8, 9). In addition to TCR, Rad26p has been shown to be involved in the nucleotide excision repair of non-transcribed regions of the genome and non-transcribed strands of genes (9).

Despite its role in DNA repair, a rad26 mutant does not display sensitivity to DNA-damaging agents such as UV, cisplatin, or X-rays. (1). Depending on the strain background, transcription-coupled repair is not abrograted in rad26 mutants (10). Rad26p has been proposed to affect transcription efficiency during TCR (11, 12, 13, 2). Rad26p forms a complex with the RNA polymerase II degradation factor Def1p when isolated from chromatin, suggesting a connection between DNA damage and ubiquitylation of RNA polymerase II (14, 15).

The RAD26 gene has a human homolog, ERCC6, that is implicated in the severe neurodegerative disorder Cockayne syndrome, type B (1, 4).

Last updated: 2007-07-12 Contact SGD

References cited on this page View Complete Literature Guide for RAD26
1) van Gool AJ, et al.  (1994) RAD26, the functional S. cerevisiae homolog of the Cockayne syndrome B gene ERCC6. EMBO J 13(22):5361-9
2) Lee SK, et al.  (2002) Yeast RAD26, a homolog of the human CSB gene, functions independently of nucleotide excision repair and base excision repair in promoting transcription through damaged bases. Mol Cell Biol 22(12):4383-9
3) Malik S and Bhaumik SR  (2012) Rad26p, a transcription-coupled repair factor, promotes the eviction and prevents the reassociation of histone H2A-H2B dimer during transcriptional elongation in vivo. Biochemistry 51(30):5873-5
4) Guzder SN, et al.  (1996) RAD26, the yeast homolog of human Cockayne's syndrome group B gene, encodes a DNA-dependent ATPase. J Biol Chem 271(31):18314-7
5) Li S and Smerdon MJ  (2002) Rpb4 and Rpb9 mediate subpathways of transcription-coupled DNA repair in Saccharomyces cerevisiae. EMBO J 21(21):5921-9
6) Teng Y and Waters R  (2000) Excision repair at the level of the nucleotide in the upstream control region, the coding sequence and in the region where transcription terminates of the Saccharomyces cerevisiae MFA2 gene and the role of RAD26. Nucleic Acids Res 28(5):1114-9
7) van den Boom V, et al.  (2002) When machines get stuck--obstructed RNA polymerase II: displacement, degradation or suicide. Bioessays 24(9):780-4
8) Li S and Smerdon MJ  (2004) Dissecting transcription-coupled and global genomic repair in the chromatin of yeast GAL1-10 genes. J Biol Chem 279(14):14418-26
9) Li S, et al.  (2006) Modulation of Rad26- and Rpb9-mediated DNA repair by different promoter elements. J Biol Chem 281(48):36643-51
10) Gregory SM and Sweder KS  (2001) Deletion of the CSB homolog, RAD26, yields Spt(-) strains with proficient transcription-coupled repair. Nucleic Acids Res 29(14):3080-6
11) You Z, et al.  (1998) 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. Mol Cell Biol 18(5):2668-76
12) Tijsterman M and Brouwer J  (1999) Rad26, the yeast homolog of the cockayne syndrome B gene product, counteracts inhibition of DNA repair due to RNA polymerase II transcription. J Biol Chem 274(3):1199-202
13) Lee SK, et al.  (2001) Requirement for yeast RAD26, a homolog of the human CSB gene, in elongation by RNA polymerase II. Mol Cell Biol 21(24):8651-6
14) Woudstra EC, et al.  (2002) A Rad26-Def1 complex coordinates repair and RNA pol II proteolysis in response to DNA damage. Nature 415(6874):929-33
15) Reid J and Svejstrup JQ  (2004) DNA damage-induced Def1-RNA polymerase II interaction and Def1 requirement for polymerase ubiquitylation in vitro. J Biol Chem 279(29):29875-8