Sequential binding of UV DNA damage binding factor and degradation of the p48 subunit as early events after UV irradiation
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چکیده
منابع مشابه
Sequential binding of UV DNA damage binding factor and degradation of the p48 subunit as early events after UV irradiation.
The UV-damaged DNA binding protein complex (UV-DDB) is implicated in global genomic nucleotide excision repair (NER) in mammalian cells. The complex consists of a heterodimer of p127 and p48. UV-DDB is defective in one complementation group (XP-E) of the heritable, skin cancer-prone disorder xeroderma pigmentosum. Upon UV irradiation of primate cells, UV-DDB associates tightly with chromatin, c...
متن کاملHuman damage-specific DNA-binding protein p48. Characterization of XPE mutations and regulation following UV irradiation.
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 th...
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Human p29 is a newly identified nuclear protein whose function is largely undetermined. We found that p29 associated with chromatin, interacted with MCM3, and localized with proliferating cell nuclear antigen foci in the S phase. Silencing of p29 using small interfering RNA duplexes reduced DNA synthesis and increased the expression of p107, a member of the RB family, and of cyclin-dependent ki...
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In the last decade an increasing number of reports are published in which UV laser micro irradiation (UVLM) is used as a new tool to generate DNA double-strand breaks (DSBs) in localized regions within single nuclei [1]. Until then only heavy ions (HI) were known for their ability to induce DSBs in strictly localized areas of cell nuclei [2], but compared to UVLM systems the experimental handli...
متن کاملp48 Activates a UV-damaged-DNA binding factor and is defective in xeroderma pigmentosum group E cells that lack binding activity.
A subset of xeroderma pigmentosum (XP) group E cells lack a factor that binds to DNA damaged by UV radiation. This factor can be purified to homogeneity as p125, a 125-kDa polypeptide. However, when cDNA encoding p125 is translated in vitro, only a small fraction binds to UV-damaged DNA, suggesting that a second factor is required for the activation of p125. We discovered that most hamster cell...
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ژورنال
عنوان ژورنال: Nucleic Acids Research
سال: 2002
ISSN: 1362-4962
DOI: 10.1093/nar/30.11.2588