Phosphoproteins of adenovirus 2

Axelrod, Nancy

doi:10.1016/0042-6822(78)90141-1

Cited by 94 publications

(45 citation statements)

References 34 publications

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“…Tryptic phosphopeptides were separated either by thin-layer chromatography [20] or by ionexchange chromatography [21]. For fingerprinting the samples were lyophilised and the remaining ammonium bicarbonate was completely removed in a vacuum oven at 60°C for 24 h. The resulting peptides were separated on cellulose thin-layer chromatography sheets as [20] with electrophoresis in 10% (v/v) acetic acid, 1% (v/v) pyridine (pH ,3.5) for 70 min at 500 V in the first dimension and chromatography in n-butanol/pyridine/acetic acid/water (37.5:25:7.5:30, by vol.)…”

Section: Separation Of S6 Phosphopeptidesmentioning

confidence: 99%

Phosphopeptide patterns of the ribosomal protein S6 following stimulation of guineapig parotid glands by secretagogues involving either cAMP or calcium as second messenger

Padel¹,

Kruppa²,

Jahn³

et al. 1983

FEBS Letters

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Stimulation of secretion in exocrine cells is associated with the incorporation of up to 3 to 4 phosphates into the ribosomal protein S6. This occurs with secretagogues involving either cAMP or free calcium as second messenger. An analysis of the phosphorylation pattern of S6 from stimulated guineapig parotid glands reveals 3 phosphopeptides (termed A,B,C). The phosphopeptide pattern was identical for cAMP‐ or calcium‐mediated stimulation, whereas phosphorylation of the S6 protein in vitro with catalytic subunit of cAMP‐dependent protein kinase resulted only in the formation of phosphopeptides A and C. Therefore, secretagogue‐mediated phosphorylation is not or not exclusively catalyzed by cAMP‐dependent protein kinase even when cAMP is the second messenger.

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Section: Separation Of S6 Phosphopeptidesmentioning

confidence: 99%

Phosphopeptide patterns of the ribosomal protein S6 following stimulation of guineapig parotid glands by secretagogues involving either cAMP or calcium as second messenger

Padel¹,

Kruppa²,

Jahn³

et al. 1983

FEBS Letters

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“…McGuire (1962) and Pryor and Steinfatt (1978) It is true that recent studies document a general weakening of party identification during the last two decades (Axelrod, 1972(Axelrod, , 1974(Axelrod, , 1978(Axelrod, , 1982(Axelrod, , 1986Boyd, 1972;Brody & Page, 1972;Goldberg, 1966;Miller & Levitan, 1976;Nie, Verba & Petrocik, 1976;Petrocik, 1980;Pomper, 1972aPomper, , 1972bPomper, , 1975Pomper & Lederman, 1980;Repass, 1971;Shapiro, 1969;Stanley, Bianco & Niemi, 1986;Weisberg & Rusk, 1970). This weakening of party identification has swelled the nonaffiliated ranks (a combination of politically apathetic and independent) to more than one-third of the electorate (Public Opinion, 1984, p. 21) and increased the extent of crossover voting (Republican identifiers who vote for Democratic candidates and vice-versa) to more than one-seventh of the electorate (Mann & Wolfinger, 1984, p. 273).…”

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confidence: 99%

Inoculation in Political Campaign Communication

1988

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The use of attack messages in political campaign communication has grown in recent years. This investigation posits a strategy of resistance to the influence of attack messages. A total of 341 initial and follow‐up treatment interviews and 392 control interviews were completed among potential voters in a U.S. Senate campaign during October 1986. We hypothesized that political campaign messages can be designed to inoculate supporters of candidates against subsequent attack messages of opposing candidates. This prediction was supported. In addition, the results supported the hypothesis that inoculation confers more resistance to subsequent attack messages among strong political party identifiers as opposed to weak identifiers, non‐identifiers, and crossovers. The results of this investigation extend the scope of inoculation theory to new domain, and at the same time, suggest a new strategic approach for candidates in political campaigns.

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“…The early region 2A gene (E2A) of human adenovirus types 2 and 5 (Ad2 and AdS) encodes a 72-kDa DNA-binding phosphoprotein (DBP) (1, 2), which is synthesized both early and late during an infectious cycle (3,4). This protein has a number of purported functions in infected cells.…”

Section: Introductionmentioning

confidence: 99%

“…This is the same domain that interacts with DNA. However, the differences in sensitivity of DBP to trypsin when bound to RNA versus DNA suggest that RNA and DNA either bind at different sites within this domain or induce different conformational changes within the protein.The early region 2A gene (E2A) of human adenovirus types 2 and 5 (Ad2 and AdS) encodes a 72-kDa DNA-binding phosphoprotein (DBP) (1, 2), which is synthesized both early and late during an infectious cycle (3,4). This protein has a number of purported functions in infected cells.…”

mentioning

confidence: 99%

Association of the adenovirus DNA-binding protein with RNA both in vitro and in vivo.

Cleghon¹,

Klessig²

1986

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

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The multifunctional DNA-binding protein (DBP) encoded by human adenovirus binds RNA. The association of purified DBP with RNA in vitro was demonstrated by using either a gel filtration or a filter binding assay. This association is sensitive to ionic strength and exhibits no apparent sequence specificity. DBP also interacts with RNA in vivo; it can be crosslinked to polyadenylylated RNA by UV-irradiation of intact cells during the late phase of adenovirus infections. The 46-kDa carboxyl-terminal domain ofDBP binds RNA in vitro and was found to be associated with polyadenylylated RNA in vivo. This is the same domain that interacts with DNA. However, the differences in sensitivity of DBP to trypsin when bound to RNA versus DNA suggest that RNA and DNA either bind at different sites within this domain or induce different conformational changes within the protein.The early region 2A gene (E2A) of human adenovirus types 2 and 5 (Ad2 and AdS) encodes a 72-kDa DNA-binding phosphoprotein (DBP) (1, 2), which is synthesized both early and late during an infectious cycle (3,4). This protein has a number of purported functions in infected cells. Analysis of DBP mutants has implicated the protein in viral DNA replication, viral early and late gene expression, and virion assembly.Studies of a DBP temperature-sensitive (ts) mutant, Ad5ts125, provides evidence of the protein's involvement in DNA replication. This mutant encodes a DBP that is thermolabile in its ability to bind to single-stranded (ss) DNA in vitro (5) and, at the nonpermissive temperature, is defective for viral DNA synthesis in vivo (6) and in vitro (7).The role of DBP in the regulation of Ad early gene expression is more controversial. DBP has been implicated in stimulating expression of early region 1B (EIB) (8) and early region 4 (E4) (9), while negatively influencing expression of early genes at intermediate and late times (10, 11). The purported negative regulation of early genes mediated by wild-type (wt) DBP appears to operate at the transcription level for E4 (12,13) and at the level of mRNA turnover for regions EIA, EIB, and probably E2A (14). However, studies by Rice and Klessig (15) (21-24). The ts, DNA replication-minus mutations are located in the 3' two-thirds of the gene, while the hr mutations map in the 5' portion ofthe gene. These functional domains appear to correspond to physical domains because digestion of purified DBP with a variety of proteases generates a C-terminal fragment of =44-46 kDa and an N-terminal fragment of -24-26 kDa (2, 25). The C-terminal fragment binds ss DNA (2) and can substitute for intact DBP in an in vitro DNA replication system (26). The N-terminal region also appears to function independently because DBP encoded by the hr mutants is able to overcome the block to late gene expression in monkey cells, even when its DNA replication function is perturbed by a ts mutation in the C-terminus (27).How the-DBP accomplishes this varied set of purported functions is still poorly understood. No enzymatic functions have...

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Phosphoproteins of adenovirus 2

Cited by 94 publications

References 34 publications

Phosphopeptide patterns of the ribosomal protein S6 following stimulation of guineapig parotid glands by secretagogues involving either cAMP or calcium as second messenger

Phosphopeptide patterns of the ribosomal protein S6 following stimulation of guineapig parotid glands by secretagogues involving either cAMP or calcium as second messenger

Inoculation in Political Campaign Communication

Association of the adenovirus DNA-binding protein with RNA both in vitro and in vivo.

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