Location of additional early gene sequences in the adenoviral chromosome

Galos, Richard S.; Williams, Jim; Binger, M H; Flint, S. J.

doi:10.1016/0092-8674(79)90334-9

Cited by 115 publications

(58 citation statements)

References 49 publications

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“…The two supernatants were combined and incubated at 25°C for 1 to 2 h in a buffer containing 15 mM KC1-75 mM NaCl-0.25% Nonidet P-40-5 mM tris(hydroxymethyl)aminomethane-chloride (pH 7.4)-0.5 mM ethylenediaminetetraacetate-1.5% sodium dodecylsulfate (SDS)-100 to 200 jig of predigested proteinase K per ml. RNA purification was as described previously (5). All solutions and glassware used with RNA were pretreated with 0.3% diethylpyrocarbonate whenever possible.…”

Section: Methodsmentioning

confidence: 99%

Post-translational regulation of the 54K cellular tumor antigen in normal and transformed cells.

Oren¹,

Maltzman²,

Levine³

1981

Mol. Cell. Biol.

484

284

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The 54K cellular tumor antigen has been translated in vitro, using messenger ribonucleic acids from simian virus 40 (SV40)-transformed cells or 3T3 cells. The in vitro 54K product could be immmunoprecipitated with SV40 tumor serum and had a peptide map that was similar, but not identical, to the in vivo product. The levels of this 54K protein in SV3T3 cells were significantly higher than those detected in 3T3 cells (D. I. H. Linzer, W. Maltzmnan, and A. J. Levine, Virology 98:308-318, 1979). In spite of this, the levels of translatable 54K messenger ribonucleic acid from 3T3 and SV3T3 cells were roughly equivalent or often greater in 3T3 cells. Pulse-chase experiments with the 54K protein from 3T3 or SV3T3 cells demonstrated that this protein, once synthesized, was rapidly degraded in 3T3 cells but was extremely stable in SV3T3 cells. Similarily, in an SV40 tsA-transformed cell line, temperature sensitive for the SV40 T-antigen, the 54K protein was rapidly turned over at the nonpermissive temperature and stable at the permissive temperature, whereas the levels of translatable 54K messenger ribonucleic acid at each temperature were roughly equal. These results demonstrate a post-translational regulation of the 54K cellular tumor antigen and suggest that this control is mediated by the SV40 large T-antigen. Animals bearing simian virus 40 (SV40)-induced tumors produce antibody to two viruscoded proteins, the large T-antigen (24) and the small t-antigen (3,20), and a cellular protein of about 54,000 molecular weight (54K) (2,9,10,12,16,23). The 54K protein has been detected in mouse 3T3 cells at about 2% the levels expressed in SV40-transformed 3T3 cells (13). SV40 infection of 3T3 cells results in a 20-to 30-fold increase in the levels of detectable 54K protein in these cells (12, 13). The SV40 A gene product, or large T-antigen, is required for this stimulation in the level of the cellular 54K protein in both virus-infected and -transformed mouse cells (13). Similar or identical proteins of 53,000 to 55,000 molecular weight have been detected in murine chemically transformed cell lines (4), embryonal carcinoma cell lines (12), spontaneously transformed cells (4; W. Maltzman, M. Oren, and A. J. Levine, Virology, in press), and lymphocytes from irradiation-induced leukemia (4). Both immunologically and chemically related 54K proteins have been detected in SV40-transformed rat, hamster, monkey, and human cell lines (6,22). Thus, the expression of high levels of the 54K protein appears to be correlated with btansformation (although not every transformed cell line expresses detectable levels of this protein), and the 54K protein appears to have been conserved, in part, over evolutionary time scales.The mechanism by which the SV40 T-antigen increases the levels of the 54K cellular protein in virus-infected or -transformed cells is at present unclear. The SV40 A gene product might stimulate the de novo synthesis of the 54K protein, as it apparently does for several celllar enzymatic activities (8,19) and the cellular ...

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Section: Methodsmentioning

confidence: 99%

Post-translational regulation of the 54K cellular tumor antigen in normal and transformed cells.

Oren¹,

Maltzman²,

Levine³

1981

Mol. Cell. Biol.

484

284

View full text Add to dashboard Cite

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“…During the early phase of productive infection of human cells by Ad2, at least eight viral genes are expressed (1)(2)(3)(4)(5); mRNA species complementary to all but one early gene, that specifying polypeptide IX (6), are spliced (refs. 7-10; unpublished observations).…”

mentioning

confidence: 99%

A small nuclear ribonucleoprotein is required for splicing of adenoviral early RNA sequences.

Yang¹,

Lerner²,

Steitz³

et al. 1981

Proc. Natl. Acad. Sci. U.S.A.

213

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A small nuclear ribonucleoprotein is required for splicing of adenoviral early RNA sequences ( Communicated by James E. Darnel, Jr., October 28, 1980 ABSTRACT The size and structure of viral RNA species synthesized in nuclei isolated during the early phase of productive infection by adenovirus type 2 have been examined by electrophoresis in denaturing polyacrylamide cells and the nuclease SI assay. The major products of transcription in vitro of early regions 1 and 2 in the adenoviral genome are processed RNA molecules that appear to be correctly spliced in isolated nuclei. Splicing of adenoviral RNA molecules is inhibited when nuclei are preincubated with antibodies from systemic lupus erythematosus patients that immunoprecipitate smail nuclear ribonucleoprotein particles.The specificity of these antibodies suggests that ribonucleoprotein particles containing Ul RNA are required for splicing of the adenoviral RNA sequences we have examined.

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“…This region has been found recently to contain early genes in addition to VA RNA [which is not poly(A)+] and the major late promoter. The two early regions, IIb (22) and an "immediate early" region (32, 43a, 46a) We have observed a reproducible decrease in virus mRNA labeling in TPA-treated cultures after the initial stimulation (Fig. 4).…”

Section: Effects Of Tumor-promoting Agents Onmentioning

confidence: 67%

Tumor promoters alter the temporal program of adenovirus replication in human cells.

Fisher¹,

Young²,

Weinstein³

et al. 1981

Mol. Cell. Biol.

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In this study we evaluated the effect of phorbol ester tumor promoters on the kinetics of adenovirus type 5 (Ad5) replication in human cells. When added at the time of infection, 12-0-tetradecanoyl-phorbol-13-acetate (TPA) accelerated the appearance of an early virus antigen (72,000-molecular-weight [72K] deoxyribonucleic acid-binding protein), the onset of viral deoxyribonucleic acid synthesis, and the production of infectious virus. The appearance of an Ad5-specific cytopathic effect (CPE) was also accelerated in infected cultures exposed to TPA, whereas phorbol, 4a-phorbol-12,13-didecanoate and 4-OmeTPA, which are inactive as tumor promoters, were ineffective in inducing this morphological change. (3,11,12,16,37,40,41,48); induction and enhancement of anchorage-independent growth in chemically transformed epidermal cells and adenovirus type 5 (Ad5)-transformed rat embryo cells (8,9,13,14,16); changes in cell surface properties (3, 7, 15,

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Location of additional early gene sequences in the adenoviral chromosome

Cited by 115 publications

References 49 publications

Post-translational regulation of the 54K cellular tumor antigen in normal and transformed cells.

Post-translational regulation of the 54K cellular tumor antigen in normal and transformed cells.

A small nuclear ribonucleoprotein is required for splicing of adenoviral early RNA sequences.

Tumor promoters alter the temporal program of adenovirus replication in human cells.

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