XPC and Human Homologs of RAD23: Intracellular Localization and Relationship to Other Nucleotide Excision Repair Complexes
The xeroderma pigmentosum syndrome complementation group C (XP-C) is due to a defect in the global genome repair subpathway of nucleotide excision repair (NER). The XPC protein is complexed with HHR23B, one of the two human homologs of the yeast NER protein, RAD23 [Masutani et al. (1994) EMBO J. 8,...
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Published in | Nucleic acids research Vol. 24; no. 13; pp. 2551 - 2559 |
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Main Authors | , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
England
Oxford University Press
01.07.1996
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Abstract | The xeroderma pigmentosum syndrome complementation group C (XP-C) is due to a defect in the global genome repair subpathway of nucleotide excision repair (NER). The XPC protein is complexed with HHR23B, one of the two human homologs of the yeast NER protein, RAD23 [Masutani et al. (1994) EMBO J. 8, 1831–1843]. 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. In contrast, we cannot detect any bound HHR23A. Thus the HHR23 proteins may have an additional function independent of XPC. The fractionation behaviour suggests that the non-bound forms of the HHR23 proteins are not necessary for the core of the NER reaction. Although both HHR23 proteins share a high level of overall homology, they migrate very differently on native gels, pointing to a difference in conformation. Gel filtration suggests the XPC-HHR23B heterodimer resides in a high MW complex. However, immunodepletion studies starting from repair-competent Manley extracts fail to reveal a stable association of a significant fraction of the HHR23 proteins or the XPC-HHR23B complex with the basal transcription/repair factor TFIIH, or with the ERCC1 repair complex. 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. |
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AbstractList | The xeroderma pigmentosum syndrome complementation group C (XP-C) is due to a defect in the global genome repair subpathway of nucleotide excision repair (NER). 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). 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. In contrast, we cannot detect any bound HHR23A. Thus the HHR23 proteins may have an additional function independent of XPC. The fractionation behaviour suggests that the non-bound forms of the HHR23 proteins are not necessary for the core of the NER reaction. Although both HHR23 proteins share a high level of overall homology, they migrate very differently on native gels, pointing to a difference in conformation. Gel filtration suggests the XPC-HHR23B heterodimer resides in a high MW complex. However, immunodepletion studies starting from repair-competent Manley extracts fall to reveal a stable association of a significant fraction of the HHR23 proteins or the XPC-HHR23B complex with the basal transcription/repair factor TFIIH, or with the ERCC1 repair complex. 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. The xeroderma pigmentosum syndrome complementation group C (XP-C) is due to a defect in the global genome repair subpathway of nucleotide excision repair (NER). The XPC protein is complexed with HHR23B, one of the two human homologs of the yeast NER protein, RAD23. 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. In contrast, we cannot detect any bound HHR23A. Thus the HHR23 proteins may have an additional function independent of XPC. The fractionation behaviour suggests that the non-bound forms of the HHR23 proteins are not necessary for the core of the NER reaction. Although both HHR23 proteins share a high level of overall homology, they migrate very differently on native gels, pointing to a difference in conformation. Gel filtration suggests the XPC-HHR23B heterodimer resides in a high MW complex. However, immunodepletion studies starting from repair-competent Manley extracts fail to reveal a stable association of a significant fraction of the HHR23 proteins or the XPC-HHR23B complex with the basal transcription/repair factor TFIIH, or with the ERCC1 repair complex. 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. The xeroderma pigmentosum syndrome complementation group C (XP-C) is due to a defect in the global genome repair subpathway of nucleotide excision repair (NER). The XPC protein is complexed with HHR23B, one of the two human homologs of the yeast NER protein, RAD23 [Masutani et al. (1994) EMBO J. 8, 1831–1843]. 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. In contrast, we cannot detect any bound HHR23A. Thus the HHR23 proteins may have an additional function independent of XPC. The fractionation behaviour suggests that the non-bound forms of the HHR23 proteins are not necessary for the core of the NER reaction. Although both HHR23 proteins share a high level of overall homology, they migrate very differently on native gels, pointing to a difference in conformation. Gel filtration suggests the XPC-HHR23B heterodimer resides in a high MW complex. However, immunodepletion studies starting from repair-competent Manley extracts fail to reveal a stable association of a significant fraction of the HHR23 proteins or the XPC-HHR23B complex with the basal transcription/repair factor TFIIH, or with the ERCC1 repair complex. 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. |
Author | Sugasawa, Kaoru Masutani, Chikahide Hoeijmakers, Jan H. J. Hanaoka, Fumio Visser, Cécile Bootsma, Dirk Eker, André Rademakers, Suzanne van der Spek, Peter J. |
AuthorAffiliation | Department of Cell Biology and Genetics, Medical Genetic Centre, Erasmus University, Rotterdam, The Netherlands |
AuthorAffiliation_xml | – name: Department of Cell Biology and Genetics, Medical Genetic Centre, Erasmus University, Rotterdam, The Netherlands |
Author_xml | – sequence: 1 givenname: Peter J. surname: van der Spek fullname: van der Spek, Peter J. organization: Department of Cell Biology and Genetics, Medical Genetic Centre, Erasmus University, PO Box 1738, 3000 DR Rotterdam, the Netherlands – sequence: 2 givenname: André surname: Eker fullname: Eker, André organization: Department of Cell Biology and Genetics, Medical Genetic Centre, Erasmus University, PO Box 1738, 3000 DR Rotterdam, the Netherlands – sequence: 3 givenname: Suzanne surname: Rademakers fullname: Rademakers, Suzanne organization: Department of Cell Biology and Genetics, Medical Genetic Centre, Erasmus University, PO Box 1738, 3000 DR Rotterdam, the Netherlands – sequence: 4 givenname: Cécile surname: Visser fullname: Visser, Cécile organization: Department of Cell Biology and Genetics, Medical Genetic Centre, Erasmus University, PO Box 1738, 3000 DR Rotterdam, the Netherlands – sequence: 5 givenname: Kaoru surname: Sugasawa fullname: Sugasawa, Kaoru organization: Department of Cell Biology and Genetics, Medical Genetic Centre, Erasmus University, PO Box 1738, 3000 DR Rotterdam, the Netherlands – sequence: 6 givenname: Chikahide surname: Masutani fullname: Masutani, Chikahide organization: Institute for Molecular and Cellular Biology, Osaka University, 1-3 Yamada-oka, Suita, Osaka 565, Japan – sequence: 7 givenname: Fumio surname: Hanaoka fullname: Hanaoka, Fumio organization: The Institute of Physical and Chemical Research (RIKEN), 2-1 Hirosawa, Wako-shi, Saitama 351-01, Japan – sequence: 8 givenname: Dirk surname: Bootsma fullname: Bootsma, Dirk organization: Department of Cell Biology and Genetics, Medical Genetic Centre, Erasmus University, PO Box 1738, 3000 DR Rotterdam, the Netherlands – sequence: 9 givenname: Jan H. J. surname: Hoeijmakers fullname: Hoeijmakers, Jan H. J. organization: Department of Cell Biology and Genetics, Medical Genetic Centre, Erasmus University, PO Box 1738, 3000 DR Rotterdam, the Netherlands |
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Snippet | The xeroderma pigmentosum syndrome complementation group C (XP-C) is due to a defect in the global genome repair subpathway of nucleotide excision repair... |
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SubjectTerms | Amino Acid Sequence Animals Cell Compartmentation Cell Nucleus - chemistry CHO Cells Cricetinae DNA Repair DNA Repair Enzymes DNA-Binding Proteins - genetics DNA-Binding Proteins - isolation & purification DNA-Binding Proteins - metabolism Fluorescent Antibody Technique HeLa Cells Humans Molecular Sequence Data Protein Binding Recombinant Proteins - isolation & purification Xeroderma Pigmentosum - chemistry |
Title | XPC and Human Homologs of RAD23: Intracellular Localization and Relationship to Other Nucleotide Excision Repair Complexes |
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