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Gene Review

RAD23B  -  RAD23 homolog B (S. cerevisiae)

Homo sapiens

Synonyms: HHR23B, HR23B, P58, UV excision repair protein RAD23 homolog B, XP-C repair-complementing complex 58 kDa protein, ...
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Disease relevance of RAD23B

  • In addition, subjects with one or 2 copies of the Val allele at codon 249 of RAD23B had a 2-fold increased risk of lung cancer (OR = 1.91, 95% CI 1.12-3.24) [1].
  • Our observations suggest that XPC-HR23B may participate in BER of G/T mismatches, thereby contributing to the suppression of spontaneous mutations that may be one of the contributory factors for the promotion of carcinogenesis in xeroderma pigmentosum genetic complementation group C patients [2].
  • We also determined that hHR23A and hHR23B could be co-purified with unique proteolytic and stress-responsive factors from human breast cancer tissues, indicating that they have unique functions in vivo [3].
  • Epigenetic silencing of the human nucleotide excision repair gene, hHR23B, in interleukin-6-responsive multiple myeloma KAS-6/1 cells [4].
  • Here we describe purification and characterization of the p68/p58 heterodimer of recombinant HIV-2 RT [5].

High impact information on RAD23B

  • Cyclobutane pyrimidine dimers (CPDs) were hardly recognized by XPC-HR23B, suggesting that additional factors may be required for CPD recognition [6].
  • In vitro experiments suggest that the mechanism involved is a combination of increased loading and turnover of OGG1 by XPC-HR23B complex [7].
  • The XPC-HR23B complex recognizes various helix-distorting lesions in DNA and initiates global genome nucleotide excision repair [2].
  • Specific antibodies raised against p58 recognize one protein in isolated nuclei and partially block 125I-labeled lamin B binding to lamin-depleted nuclear membranes [8].
  • hHR23B was originally isolated as a component of a protein complex that specifically complements nucleotide excision repair (NER) defects of xeroderma pigmentosum group C cell extracts in vitro and was identified as one of two human homologs of the Saccharomyces cerevisiae NER gene product Rad23 [9].

Biological context of RAD23B


Anatomical context of RAD23B

  • Expression of a novel RAD23B mRNA splice variant in the human testis [10].
  • Intriguingly, hHR23B showed the inhibitory effect on the degradation of (125)I-lysozyme in the rabbit reticulocyte lysate. hHR23 proteins thus appear to associate with 26 S proteasome in vivo [13].
  • However, when a cholesterol-substituted oligonucleotide was used as substrate, excision occurred in the absence of the XPC-HHR23B complex, reminiscent of transcription-coupled repair in the XP-C mutant cell line [14].
  • Surprisingly, no reduction in repair capacity was observed in primary human fibroblasts that overexpressed GFP-polyQ, a polypeptide that induces HR23B-positive inclusions in these transfected cells [15].
  • Interestingly, HR23B did not significantly accumulate in tau-positive aggregates (neurofibrillary tangles) from AD patients while ubiquitin did [15].

Associations of RAD23B with chemical compounds

  • Using heparin chromatography, gel filtration and native gel electrophoresis we demonstrate that the majority of HHR23B is in a free, non-complexed form, and that a minor fraction is tightly associated with XPC [16].
  • Threonine-79 contributed to the weak proteasome-binding property of hHR23A, and its conversion to proline (T79P), which is the residue present in hHR23B, increased proteasome interaction [3].
  • This hypermethylation was significantly abated by Zebularine, a potent demethylating agent, with a consequent increase in the hHR23B mRNA level [4].
  • The XPC-HHR23B complex is required for excision of thymine dimers from DNA in a human excision nuclease system reconstituted from purified proteins [17].
  • A strong preference of XPC-hHR23B for UV- and cisplatin-damaged DNA has previously been demonstrated using equilibrium binding assays [18].

Physical interactions of RAD23B

  • The XPC protein is complexed with HHR23B, one of the two human homologs of the yeast NER protein, RAD23 (Masutani at al. (1994) EMBO J. 8, 1831-1843) [16].

Regulatory relationships of RAD23B

  • In a reconstituted repair system, hHR23B stimulated XPC activity tenfold [19].

Other interactions of RAD23B

  • Consistent with a function in repair or DNA/chromatin metabolism, immunofluorescence studies show all XPC, HHR23B and (the free) HHR23A to reside in the nucleus [16].
  • XPC-C exhibits binding characteristics of the full-length protein, including stimulation of DNA binding by physical interaction with RAD23B and CETN2 [20].
  • Although human Rad23 proteins (hHR23A and hHR23B) have redundant roles in DNA repair, we determined they formed distinct interactions with proteasomes and multiubiquitinated proteins, but similar binding to Ataxin-3 [3].
  • Subsequent removal of this drug and supplementation with IL-6 in the culture medium re-established DNA hypermethylation of the hHR23B gene and silencing of mRNA expression levels [4].
  • DNA duplexes containing photoreactive analogues were used to analyze the interaction of XPC-HR23B, RPA, and XPA with damaged DNA using the photocrosslinking assay [21].

Analytical, diagnostic and therapeutic context of RAD23B


  1. Polymorphisms in the DNA nucleotide excision repair genes and lung cancer risk in Xuan Wei, China. Shen, M., Berndt, S.I., Rothman, N., Demarini, D.M., Mumford, J.L., He, X., Bonner, M.R., Tian, L., Yeager, M., Welch, R., Chanock, S., Zheng, T., Caporaso, N., Lan, Q. Int. J. Cancer (2005) [Pubmed]
  2. Xeroderma pigmentosum group C protein interacts physically and functionally with thymine DNA glycosylase. Shimizu, Y., Iwai, S., Hanaoka, F., Sugasawa, K. EMBO J. (2003) [Pubmed]
  3. Evidence for distinct functions for human DNA repair factors hHR23A and hHR23B. Chen, L., Madura, K. FEBS Lett. (2006) [Pubmed]
  4. Epigenetic silencing of the human nucleotide excision repair gene, hHR23B, in interleukin-6-responsive multiple myeloma KAS-6/1 cells. Peng, B., Hodge, D.R., Thomas, S.B., Cherry, J.M., Munroe, D.J., Pompeia, C., Xiao, W., Farrar, W.L. J. Biol. Chem. (2005) [Pubmed]
  5. Characterization of the p68/p58 heterodimer of human immunodeficiency virus type 2 reverse transcriptase. Fan, N., Rank, K.B., Poppe, S.M., Tarpley, W.G., Sharma, S.K. Biochemistry (1996) [Pubmed]
  6. A multistep damage recognition mechanism for global genomic nucleotide excision repair. Sugasawa, K., Okamoto, T., Shimizu, Y., Masutani, C., Iwai, S., Hanaoka, F. Genes Dev. (2001) [Pubmed]
  7. New functions of XPC in the protection of human skin cells from oxidative damage. D'Errico, M., Parlanti, E., Teson, M., de Jesus, B.M., Degan, P., Calcagnile, A., Jaruga, P., Bjørås, M., Crescenzi, M., Pedrini, A.M., Egly, J.M., Zambruno, G., Stefanini, M., Dizdaroglu, M., Dogliotti, E. EMBO J. (2006) [Pubmed]
  8. A lamin B receptor in the nuclear envelope. Worman, H.J., Yuan, J., Blobel, G., Georgatos, S.D. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  9. Identification and characterization of XPC-binding domain of hHR23B. Masutani, C., Araki, M., Sugasawa, K., van der Spek, P.J., Yamada, A., Uchida, A., Maekawa, T., Bootsma, D., Hoeijmakers, J.H., Hanaoka, F. Mol. Cell. Biol. (1997) [Pubmed]
  10. Expression of a novel RAD23B mRNA splice variant in the human testis. Huang, X., Wang, H., Xu, M., Lu, L., Xu, Z., Li, J., Zhou, Z., Sha, J. J. Androl. (2004) [Pubmed]
  11. Centrosome protein centrin 2/caltractin 1 is part of the xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repair. Araki, M., Masutani, C., Takemura, M., Uchida, A., Sugasawa, K., Kondoh, J., Ohkuma, Y., Hanaoka, F. J. Biol. Chem. (2001) [Pubmed]
  12. Studies on the intracellular localization of hHR23B. Katiyar, S., Lennarz, W.J. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  13. Interaction of hHR23 with S5a. The ubiquitin-like domain of hHR23 mediates interaction with S5a subunit of 26 S proteasome. Hiyama, H., Yokoi, M., Masutani, C., Sugasawa, K., Maekawa, T., Tanaka, K., Hoeijmakers, J.H., Hanaoka, F. J. Biol. Chem. (1999) [Pubmed]
  14. Reaction mechanism of human DNA repair excision nuclease. Mu, D., Hsu, D.S., Sancar, A. J. Biol. Chem. (1996) [Pubmed]
  15. The DNA repair-ubiquitin-associated HR23 proteins are constituents of neuronal inclusions in specific neurodegenerative disorders without hampering DNA repair. Bergink, S., Severijnen, L.A., Wijgers, N., Sugasawa, K., Yousaf, H., Kros, J.M., van Swieten, J., Oostra, B.A., Hoeijmakers, J.H., Vermeulen, W., Willemsen, R. Neurobiol. Dis. (2006) [Pubmed]
  16. XPC and human homologs of RAD23: intracellular localization and relationship to other nucleotide excision repair complexes. van der Spek, P.J., Eker, A., Rademakers, S., Visser, C., Sugasawa, K., Masutani, C., Hanaoka, F., Bootsma, D., Hoeijmakers, J.H. Nucleic Acids Res. (1996) [Pubmed]
  17. Overproduction, purification, and characterization of the XPC subunit of the human DNA repair excision nuclease. Reardon, J.T., Mu, D., Sancar, A. J. Biol. Chem. (1996) [Pubmed]
  18. Pre-steady-state binding of damaged DNA by XPC-hHR23B reveals a kinetic mechanism for damage discrimination. Trego, K.S., Turchi, J.J. Biochemistry (2006) [Pubmed]
  19. Stable binding of human XPC complex to irradiated DNA confers strong discrimination for damaged sites. Batty, D., Rapic'-Otrin, V., Levine, A.S., Wood, R.D. J. Mol. Biol. (2000) [Pubmed]
  20. Biochemical and structural domain analysis of xeroderma pigmentosum complementation group C protein. Bunick, C.G., Miller, M.R., Fuller, B.E., Fanning, E., Chazin, W.J. Biochemistry (2006) [Pubmed]
  21. Crosslinking of the NER damage recognition proteins XPC-HR23B, XPA and RPA to photoreactive probes that mimic DNA damages. Maltseva, E.A., Rechkunova, N.I., Gillet, L.C., Petruseva, I.O., Schärer, O.D., Lavrik, O.I. Biochim. Biophys. Acta (2007) [Pubmed]
  22. Chromosomal localization of three repair genes: the xeroderma pigmentosum group C gene and two human homologs of yeast RAD23. van der Spek, P.J., Smit, E.M., Beverloo, H.B., Sugasawa, K., Masutani, C., Hanaoka, F., Hoeijmakers, J.H., Hagemeijer, A. Genomics (1994) [Pubmed]
  23. HHR23B, a human Rad23 homolog, stimulates XPC protein in nucleotide excision repair in vitro. Sugasawa, K., Masutani, C., Uchida, A., Maekawa, T., van der Spek, P.J., Bootsma, D., Hoeijmakers, J.H., Hanaoka, F. Mol. Cell. Biol. (1996) [Pubmed]
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