Localization of the adenovirus E1Aa protein, a positive-acting transcriptional factor, in infected cells infected cells.

Feldman, Lawrence T.; Nevins, J R

doi:10.1128/mcb.3.5.829

Cited by 102 publications

(65 citation statements)

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“…These results are in general agreement with a number of recently published reports Yee et al, 1983;Feldman & Nevins, 1983) in which it was shown, using mainly immunofluorescence techniques, that in Ad-5-infected cells most of the Ela proteins and the Elb 58K protein were located in the nucleus and cytoplasm. Previous immunofluorescence studies in our laboratory using TBS have also suggested a distribution of Ad-12 52K and 41K proteins similar to that obtained with the subcellular fractionation (P. H. Gallimore, unpublished results).…”

Section: Discussionsupporting

confidence: 82%

“…However, our inability to demonstrate significant levels of 41K protein associated with the chromatin possibly indicates that such an interaction may not occur in ~,ivo. This is supported by the observations of Feldman & Nevins (1983) who found in Ad-5-infected cells that the portion of the Ela protein present in the nucleus co-purifies with the nuclear matrix.…”

Section: Discussionsupporting

confidence: 78%

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Adenovirus Type 12 Early Region 1 Proteins: A Study of their Subcellular Localization and Protein-Protein Interactions

Grand

Gallimore

1984

Journal of General Virology

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SUMMARYSubcellular fractionation of rat and human cells transformed by the adenovirus type 12 (Ad-12) EcoRI-C DNA fragment showed that the 41000 mol. wt. (41K) Ela and 52K Elb proteins were present in the nucleus and cytoplasm at approximately equal concentrations. The 18K El b protein was associated with the nuclear, mitochondrial, lysosomal and membrane fractions. The 41K E la protein was also associated with various cytoskeletal structures (probably microtubules and 10 nm filaments) in Ad-12-transformed cells. The Ad-12 E1 41K and 52K proteins have been partially purified from transformed and infected cells. Using these preparations the 52K protein has been shown to exist under non-reducing conditions and probably in vivo as a 100K dimer stabilized by intermolecular disulphide bonds. The 41K protein bound strongly to histones H1 and H4 but much more weakly to H2A, H2B and H3. It did not interact with other comparable basic proteins or with the cytoskeletal components actin, tropomyosin and calmodulin. Although the 41K Ela protein bound to histones in vitro it is probable that such an interaction may not occur in vivo as very little of the adenovirus protein co-purified with chromatin from transformed cells. None of the Ad-12 E1 proteins showed any ATPase or protein kinase activity.

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Section: Discussionsupporting

confidence: 82%

Section: Discussionsupporting

confidence: 78%

Adenovirus Type 12 Early Region 1 Proteins: A Study of their Subcellular Localization and Protein-Protein Interactions

Grand

Gallimore

1984

Journal of General Virology

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“…These include the internal chromosomal scaffold proteins (29), the well-characterized lamin proteins which underlie the nuclear envelope (20)(21)(22), tight DNA-binding proteins (8,35), and certain DNA tumor virus-transforming proteins, such as simian virus 40 and polyomavirus large T antigens (9,40,44), adenovirus ElAa (19), and herpesvirus ICP8 proteins (33). Our .…”

Section: Downloaded Frommentioning

confidence: 99%

V-myc- and c-myc-encoded proteins are associated with the nuclear matrix.

Eisenman¹,

Tachibana²,

Abrams³

et al. 1985

Mol. Cell. Biol.

223

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A series of extraction procedures were applied to avian nuclei which allowed us to define three types of association of v-myc-and c-myc-encoded proteins with nuclei: (i) a major fraction (60 to 90%) which is retained in DNA-and RNA-depleted nuclei after low-and high-salt extraction, (ii) a small fraction (1%) released during nuclease digestion of DNA in intact nuclei in the presence of low-salt buffer, and (iii) a fraction of myc protein (<10%) extractable with salt or detergents and found to have affinity for both single-and double-stranded DNA. Immunofluorescence analysis with anti-myc peptide sera on cells extracted sequentially with nucleases and salts confirmed the idea that myc proteins were associated with a complex residual nuclear structure (matrix-lamin fraction) which also contained avian nuclear lamin protein. Dispersal of myc proteins into the cytoplasm was found to occur during mitosis. Both c-myc and v-myc proteins were associated with the matrix-lamin, suggesting that the function of myc may relate to nuclear structural organization.Recent evidence indicates that the proteins encoded by retroviral oncogenes fall into two classes with respect to their predominant subcellular localizations. The proteins encoded by the rather diverse oncogene families showing various degrees of relatedness to src or ras have been known for some time to be present in the cytoplasmic or plasma membrane compartments or in both. Recently it has been shown that the protein products of the myc, myb, and fos genes have a nuclear localization (37). Although gross subcellular location provides only a hint as to oncogene function, the nuclear localization of myc proteins (1,4,16,23) is especially intriguing in light of evidence suggesting that myc may relate to cell growth control (10,28,32,38). In addition it appears that alterations at the myc locus may be underlying events in many lymphoid and at least several nonlymphoid neoplasms in birds, rodents, and humans. The role that myc plays in these events, however, is unknown.In principle, three classes of myc-related proteins can be considered: the v-myc-encoded proteins produced by the avian acute leukemia viruses; the c-myc protein synthesized after translocation, amplification, or promoter insertion in the vicinity of the c-myc allele; and the c-myc protein produced by an unaltered normal c-myc gene. In the avian system the group of acute leukemia viruses which possess the myc oncogene synthesize their v-myc proteins as either fusion products containing viral structural protein regions (usually derived from the gag gene which specifies the internal structural protein precursor) linked to v-myc protein regions (MC29 pjj0gag-mYc, CMII p9fgag-myc OK10 P200gag-pol-myc) or as v-myc proteins apparently not linked to any other viral proteins (OK10 p62v-mYc; MH2 p61/63vmYc) (4,23,26). In avian bursal lymphoma cell lines, in which c-myc transcription has been increased due to proximal integration of a retroviral long terminal repeat, a 62,000-dalton protein has been identified as t...

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“…We speculate that p64 and p67 may be derived from these RNA species by an internal splice site within one of the coding exons in a manner similar to that described for the adenovirus Ela gene (42). Interestingly, Ela proteins also have short half-lives of 30 to 45 min (K. R. Spindler and A. J. Berk, submitted for publication) and are also tightly bound to the cell nucleus (16).…”

mentioning

confidence: 99%

Proteins encoded by the human c-myc oncogene: differential expression in neoplastic cells.

Hann¹,

Eisenman²

1984

Mol. Cell. Biol.

474

300

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To examine myc protein products in the wide variety of human tumor cells having alterations of the c-myc locus, we have prepared an antiserum against a synthetic peptide corresponding to the predicted C-terminal sequence of the human c-myc protein. This antiserum (anti-hu-myc 12C) specifically precipitated two proteins of 64 and 67 kilodaltons in quantities ranging from low levels in normal fibroblasts to 10-fold-higher levels in Epstein-Barr virus-immortalized and Burkitt's lymphoma cell lines, to 20-to 60-fold-higher levels in cell lines having amplified c-myc. The p64 and p67 proteins were found to be highly related by partial V8 proteolytic mapping, and both were demonstrated to be encoded by the c-myc oncogene, using hybrid-selected translation of myc-specific RNA. In addition, the p64 protein was specifically precipitated from cells transfected with a translocated c-myc gene. Both p64 and p67 were found to be nuclear phosphoproteins with extremely short half-lives. In tumor cell lines having alterations at the c-myc locus due to amplification or translocation, we observed a significant change in the expression of p64 relative to p67 when compared with normal or EpsteinBar virus-immortalized cells.

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Localization of the adenovirus E1Aa protein, a positive-acting transcriptional factor, in infected cells infected cells.

Cited by 102 publications

References 50 publications

Adenovirus Type 12 Early Region 1 Proteins: A Study of their Subcellular Localization and Protein-Protein Interactions

Adenovirus Type 12 Early Region 1 Proteins: A Study of their Subcellular Localization and Protein-Protein Interactions

V-myc- and c-myc-encoded proteins are associated with the nuclear matrix.

Proteins encoded by the human c-myc oncogene: differential expression in neoplastic cells.

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