Human Damage-specific DNA-binding Protein p48
Open accessAbstract
Damage-specific DNA binding (DDB) activity purifies from HeLa cells as a heterodimer (p127 and p48) and is absent from cells of a subset (Ddb(-)) of xeroderma pigmentosum Group E (XPE) patients. Each subunit was overexpressed in insect cells and purified. Both must be present for the damaged DNA band shift characteristic of the HeLa heterodimer. However, overexpressed p48 peptides containing the mutations found in three Ddb(-) XPE strains are inactive, and wild type p48 restores DDB activity to extracts from a fourth XPE Ddb(-) strain, GM01389, in which compound heterozygous mutations in DDB2 (p48) lead to a L350P change from one allele and a Asn-349 deletion from the other. Although these results indicate that these mutations are each responsible for the loss of DDB activity, they do not affect nuclear localization of p48. In normal fibroblasts, a 4-fold increase in p48 mRNA amount was observed 38 h after UV irradiation, preceding a similar elevation in p48 protein and DDB activity at 48 h, implying that p48 limits DDB activity in vivo. Because DNA repair is virtually complete before 48 h, a role for DDB other than DNA repair is suggested.
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GM01389 cells defective in DDB2 carry a DDB2 mutation that impairs complex formation with DDB1 and consequently the formation of a functional DDB-XPC complex.
“DDB2-defective GM01389 cells carry mutation in DDB2 [52], which affects complex formation with DDB1 [58], and consequently the formation of functional DDB-XPC complex.”
From NER initiation factors, DDB2 and XPC, regulate UV radiation response by recruiting ATR and ATM kinases to DNA damage sites (2013) · cites this paper as [52]
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References 37 · Cited by 137
Research works printed but not linked: 2
- Kazantsev, A., Mu, D., Nichols, A. F., Zhao, X., Linn, S., and Sancar, A. (1996) Proc. Natl. Acad. Sci. U. S. A. 93, 5014 -5018
- Keeney, S., Eker, A. P. M., Brody, T., Vermeulen, W., Bootsma, D., Hoeijmakers, J. H. J., and Linn, S. (1994) Proc. Natl. Acad. Sci. U. S. A. 91, 4053-4056
- Authors
- Nichols, A. F., Itoh, T., Graham, J. A., Liu, W., Yamaizumi, M., & Linn, S.
- Affiliations
- University of California, Berkeley (US)
- Institute of Molecular Embryology and Genetics, Kumamoto University (JP)
- Corresponding author
- Linn, Stuart
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-07
- Volume
- 275
- Issue
- 28
- Pages
- 21422-21428
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1997871326
- Cited by
- 137
- References
- 37
- Citations by year
- 2025: 1 · 2023: 2 · 2022: 1 · 2021: 1 · 2020: 3 · 2019: 1 · 2018: 2 · 2017: 2 · 2016: 6 · 2015: 6 · 2014: 3 · 2013: 4 · 2012: 5
- FWCI
- 4.22
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- U.S. Department of Energy
- National Institutes of Health
- National Institute of Environmental Health Sciences (P30-ES08196)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Health Sciences › Medicine › Pathology and Forensic Medicine › Genetic factors in colorectal cancer
- Keywords
- p48, DDB2, DNA damage response, UV irradiation, DNA repair, compound heterozygosity, nuclear localization, HeLa cells
- MeSH terms
- Animals, DNA-Binding Proteins, Fibroblasts, Gene Expression Regulation, HeLa Cells, Heterozygote, Humans, Mutation, Recombinant Proteins, RNA, Messenger, Transcription, Genetic, Transfection, Ultraviolet Rays, Xeroderma Pigmentosum, Point Mutation, Sequence Deletion, Sequence Analysis, DNA, Spodoptera, Dimerization, Amino Acid Substitution
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