Title Identification of UHRF1/2 as new N-methylpurine DNA glycosylase-interacting proteins
Authors Liang, Chao
Zhang, Xueli
Song, Shanshan
Tian, Chunyan
Yin, Yuxin
Xing, Guichun
He, Fuchu
Zhang, Lingqiang
Affiliation Anhui Med Univ, Dept Cell Biol, Hefei 230032, Anhui, Peoples R China.
Beijing Inst Radiat Med, Beijing Proteome Res Ctr, State Key Lab Prote, Beijing 100850, Peoples R China.
Univ So Calif, Dept Mol Microbiol & Immunol, Los Angeles, CA 90033 USA.
Peking Univ, Dept Pathol, Sch Basic Med Sci, Beijing 100191, Peoples R China.
Keywords MPG
UHRF1
UHRF2
IP/MS
Protein interaction
BASE EXCISION-REPAIR
CELL-CYCLE ARREST
ALKYLATING-AGENTS
CANCER
METHYLATION
SENSITIVITY
ICBP90
TARGET
DNMT1
LINKS
Issue Date 2013
Publisher 生物化学与生物物理学研究通讯
Citation BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS.2013,433,(4),415-419.
Abstract N-methylpurine DNA glycosylase (MPG), a DNA repair enzyme, functions in the DNA base excision repair (BER) pathway. Aberrant over-expression of MPG in various cancers suggests an important role of MPG in carcinogenesis. Identification of MPG-interacting proteins will help to dissect the molecular link between MPG and cancer development. In the present study, using immunoprecipitation coupled with mass spectrometry (IP/MS), we screened ubiquitin-like, containing PHD and RING finger domains 1 (UHRF1), an essential protein required for the maintenance of DNA methylation, as a MPG-interacting protein. Endogenous co-immunoprecipitation assay in cancer cells confirmed that UHRF1 interacted with MPG in a p53 status-independent manner. Confocal microscopy showed that endogenous MPG and UHRF1 were co-localized in the nucleoplasm. Furthermore, co-immunoprecipitation assay indicated that UHRF2, the homolog of UHRF1, could also interact with MPG. These results show that MPG and the UHRF family of proteins interact, thus providing a functional linkage between MPG and UHRF1/2. (C) 2013 Elsevier Inc. All rights reserved.
URI http://hdl.handle.net/20.500.11897/225360
ISSN 0006-291X
DOI 10.1016/j.bbrc.2013.02.126
Indexed SCI(E)
Appears in Collections: 基础医学院

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