Dynamic redistribution of nuclear matrix proteins by adenovirus infection.
We analyzed the redistribution of nuclear proteins, PML protein, Ku70/Ku80, a putative spliceosome associated protein, pNMM102 and a nucleolar proliferating antigen, p120 after adenovirus 5 (Ad5) infection using immunofluorescent staining. These proteins remained after in situ fractionation. PML was located at irregular bars 6 h after infection from fine dots of uninfected cells. Distribution pattern of PML was not changed throughout the course of infection. Internal nuclear matrix network composed of Ku protein became much coarser in interphase cells at 12 h after infection. Ku protein was clumped at 18 h after infection, where EIA protein was colocalized. Speckles and interconnecting fibrils recognized by monoclonal antibody NMM102 disappeared early after infection, and reappeared at 18 h after infection in various patterns. The number and staining intensity of p120 containing domains increased markedly in early replication phase, and their shape became irregular with a few fine dots. A few Ad5 infected cells revealed diffuse nucleoplasmic as well as nucleolar p120 in late replication phase. Redistribution of four different nuclear matrix proteins by Ad5 infection indicates that the nuclear matrix is dynamically involved in gene expression.
Yu
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Department of Pathology, University of Ulsan College of Medicine, Seoul 138-736, Korea.
Joo
Y K
YK
Lee
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I
D000257:Adenoviridae Infections / Q000378:metabolism*; D017500:Adenovirus E1A Proteins / Q000378:metabolism; D000911:Antibodies, Monoclonal; D034961:Antigens, Nuclear; D002458:Cell Fractionation; D004265:DNA Helicases; D004268:DNA-Binding Proteins / Q000378:metabolism; D019084:Fluorescent Antibody Technique, Indirect; D006801:Humans; D000072200:Ku Autoantigen; D009363:Neoplasm Proteins / Q000378:metabolism; D009687:Nuclear Proteins / Q000378:metabolism*; D000071156:Promyelocytic Leukemia Protein; D016601:RNA-Binding Proteins / Q000378:metabolism; D017381:Spliceosomes / Q000276:immunology / Q000378:metabolism; D014157:Transcription Factors / Q000378:metabolism; D014407:Tumor Cells, Cultured; D025521:Tumor Suppressor Proteins; D012359:tRNA Methyltransferases
D017500:Adenovirus E1A Proteins; D000911:Antibodies, Monoclonal; D034961:Antigens, Nuclear; D004268:DNA-Binding Proteins; D009363:Neoplasm Proteins; D009687:Nuclear Proteins; D000071156:Promyelocytic Leukemia Protein; D016601:RNA-Binding Proteins; D014157:Transcription Factors; D025521:Tumor Suppressor Proteins; C070576:PML protein, human; C065028:NOP2 protein, human; D012359:tRNA Methyltransferases; D004265:DNA Helicases; C106893:XRCC5 protein, human; C000606509:Xrcc6 protein, human; D000072200:Ku Autoantigen