Oncotarget

Research Papers:

The proteomic investigation reveals interaction of mdig protein with the machinery of DNA double-strand break repair

Wei Wang, Yongju Lu, Paul M. Stemmer, Xiangmin Zhang, Yongyi Bi, Zhengping Yi and Fei Chen _

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Oncotarget. 2015; 6:28269-28281. https://doi.org/10.18632/oncotarget.4961

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Abstract

Wei Wang1,2, Yongju Lu1, Paul M. Stemmer3, Xiangmin Zhang1, Yongyi Bi2, Zhengping Yi1 and Fei Chen1

1 Department of Pharmaceutical Sciences, Eugene Applebaum College of Pharmacy and Health Sciences, Wayne State University, Detroit, MI, USA

2 School of Public Health, Wuhan University, Wuhan, Hubei, P.R. China

3 The Proteomics Core and Institute of Environmental Health Sciences, School of Medicine, Wayne State University, Detroit, MI, USA

Correspondence to:

Fei Chen, email:

Keywords: mdig, DNA repair, NHEJ, XRCC5, XRCC6

Received: June 08, 2015 Accepted: July 03, 2015 Published: July 22, 2015

Abstract

To investigate how mineral dust-induced gene (mdig, also named as mina53, MINA, or NO52) promotes carcinogenesis through inducing active chromatin, we performed proteomics analyses for the interacting proteins that were co-immunoprecipitated by anti-mdig antibody from either the lung cancer cell line A549 cells or the human bronchial epithelial cell line BEAS-2B cells. On SDS-PAGE gels, three to five unique protein bands were consistently observed in the complexes pulled-down by mdig antibody, but not the control IgG. In addition to the mdig protein, several DNA repair or chromatin binding proteins, including XRCC5, XRCC6, RBBP4, CBX8, PRMT5, and TDRD, were identified in the complexes by the proteomics analyses using both Orbitrap Fusion and Orbitrap XL nanoESI-MS/MS in four independent experiments. The interaction of mdig with some of these proteins was further validated by co-immunoprecipitation using antibodies against mdig and its partner proteins, respectively. These data, thus, provide evidence suggesting that mdig accomplishes its functions on chromatin, DNA repair and cell growth through interacting with the partner proteins.


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