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Human NTH1 Physically Interacts With p53 and Proliferating Cell Nuclear Antigen

Human NTH1 Physically Interacts With p53 and Proliferating Cell Nuclear Antigen

Masaki Oyama, Mitsuo Wakasugi, Takashi Hama, Hatsuho Hashidume, Yasutaka Iwakami, Rika Imai, Sanae Hoshino, Hiroshi Morioka, Yasuhito Ishigaki, Osamu Nikaido, Tsukasa Matsunaga

Biochem Biophys Res Commun. 2004 Aug 13;321(1):183-91.

PMID: 15358233

Abstract:

Thymine glycol (Tg) is one of predominant oxidative DNA lesions caused by ionizing radiation and other oxidative stresses. Human NTH1 is a bifunctional enzyme with DNA glycosylase and AP lyase activities and removes Tg as the first step of base excision repair (BER). We have searched for the factors interacting with NTH1 by using a pull-down assay and found that GST-NTH1 fusion protein precipitates proliferating cell nuclear antigen (PCNA) and p53 as well as XPG from human cell-free extracts. GST-NTH1 also bound to recombinant FLAG-tagged XPG, PCNA, and (His)6-tagged p53 proteins, indicating direct protein-protein interaction between those proteins. Furthermore, His-p53 and FLAG-XPG, but not PCNA, stimulated the Tg DNA glycosylase/AP lyase activity of GST-NTH1 or NTH1. These results provide an insight into the positive regulation of BER reaction and also suggest a possible linkage between BER of Tg and other cellular mechanisms.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42415015	PCNA, His tagged human			Price

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