title: The proteomic investigation reveals interaction of mdig protein with the machinery of DNA double-strand break repair.
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.
authors: Department of Pharmaceutical Sciences, Eugene Applebaum College of Pharmacy and Health Sciences, Wayne State University, Detroit, MI, USA.|School of Public Health, Wuhan University, Wuhan, Hubei, P.R. China.
authors: Wei
authors: W
authors: Wang
authors: Department of Pharmaceutical Sciences, Eugene Applebaum College of Pharmacy and Health Sciences, Wayne State University, Detroit, MI, USA.
authors: Yongju
authors: Y
authors: Lu
authors: The Proteomics Core and Institute of Environmental Health Sciences, School of Medicine, Wayne State University, Detroit, MI, USA.
authors: Paul M
authors: PM
authors: Stemmer
authors: Department of Pharmaceutical Sciences, Eugene Applebaum College of Pharmacy and Health Sciences, Wayne State University, Detroit, MI, USA.
authors: Xiangmin
authors: X
authors: Zhang
authors: School of Public Health, Wuhan University, Wuhan, Hubei, P.R. China.
authors: Yongyi
authors: Y
authors: Bi
authors: Department of Pharmaceutical Sciences, Eugene Applebaum College of Pharmacy and Health Sciences, Wayne State University, Detroit, MI, USA.
authors: Zhengping
authors: Z
authors: Yi
authors: Department of Pharmaceutical Sciences, Eugene Applebaum College of Pharmacy and Health Sciences, Wayne State University, Detroit, MI, USA.
authors: Fei
authors: F
authors: Chen
mesh_terms: D000595:Amino Acid Sequence; D000903:Antibiotics, Antineoplastic / Q000494:pharmacology; D034961:Antigens, Nuclear / Q000378:metabolism; D002460:Cell Line; D045744:Cell Line, Tumor; D053903:DNA Breaks, Double-Stranded / Q000187:drug effects; D004265:DNA Helicases / Q000378:metabolism; D004260:DNA Repair; D004268:DNA-Binding Proteins / Q000378:metabolism; D049308:Dioxygenases; D004591:Electrophoresis, Polyacrylamide Gel; D056466:Histone Demethylases; D006801:Humans; D000072200:Ku Autoantigen; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000378:metabolism*; D010692:Phleomycins / Q000494:pharmacology; D020543:Proteome / Q000378:metabolism*; D040901:Proteomics / Q000379:methods*; D056505:Retinoblastoma-Binding Protein 4 / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D053719:Tandem Mass Spectrometry / Q000379:methods
chemical_list: D000903:Antibiotics, Antineoplastic; D034961:Antigens, Nuclear; D004268:DNA-Binding Proteins; D009687:Nuclear Proteins; D010692:Phleomycins; D020543:Proteome; C082637:RBBP4 protein, human; D056505:Retinoblastoma-Binding Protein 4; D049308:Dioxygenases; D056466:Histone Demethylases; C466777:RIOX2 protein, human; D004265:DNA Helicases; C106893:XRCC5 protein, human; C000606509:Xrcc6 protein, human; D000072200:Ku Autoantigen
keywords: DNA repair; NHEJ; XRCC5; XRCC6; mdig