ADP-ribosylation in in vitro Systems Synthesizing Adenovirus DNA

Goding, Colin R.; Shaw, Charles R.; Blair, G. Eric; Russell, W. C.

doi:10.1099/0022-1317-64-2-477

Cited by 10 publications

(2 citation statements)

References 27 publications

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“…Although [32 P]ADP-ribose was incorporated into both normal cellular and viral-induced infected-cell proteins, no incorporation was found in any member of this family of proteins. This distinguishes these proteins from the herpes simplex virus type 1 IE polypeptide Vmwl75/ICP4 (27), the SV40 large T antigen (15), and the adenovirus T antigen (12), in which this type of modification has been identified.…”

Section: Resultsmentioning

confidence: 99%

Posttranscriptional regulation of a class of human cytomegalovirus phosphoproteins encoded by an early transcription unit

Wright

Spector

1989

J Virol

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We have further characterized and determined the origins of a family of nuclear phosphoproteins of 84, 50, 43, and 34 kilodaltons (kDa) encoded by a class of early transcripts arising from the adjacent EcoRI fragments R and d (map units 0.682 to 0.713) of the strain AD169 human cytomegalovirus genome. These RNAs have a complex spliced structure with common 5' and internal exons and alternative 3' exons with coterminal 3' ends. At early times, two fully processed species of 2.1 and 2.2 kilobases (kb) predominated. As the infection progressed to late times, there was a decrease in splicing of the RNA, generating larger transcripts 2.5 to 2.65 kb in size, which corresponded to the species which had spliced out only the first intron, as well as the completely unspliced transcript. We previously reported that the 34-kDa protein could be derived from a transcript which had failed to splice out the first intron (D. A. Wright, S. I. Staprans, and D. H. Spector, J. Virol. 62:331-340, 1988), but the origin of the other proteins was unclear. cDNA cloning has shown that the 2.1-, 2.2-, and 2.5-kb RNAs encode the 50-, 43-, and 84-kDa proteins, respectively. The shift in the splicing pattern of these RNAs with time revealed a posttranscriptional control mechanism which results in the differential accumulation of individual proteins within this family of nuclear phosphoproteins. Expression of the 84-, 43-, and 34-kDa proteins correlated well with the steady-state concentrations of their respective mRNAs. The 50-kDa protein, however, was not expressed in abundance until late times, despite the presence of the 2.1-kb mRNA in the cytoplasm at early times, suggesting a secondary level of posttranscriptional regulation for this protein. Full expression of the RNAs and proteins was dependent on continuing viral DNA synthesis. Accumulation of the 50-kDa protein was found to be particularly sensitive to the state of viral DNA replication and could not be detected after inhibition of replication. Further analysis of these proteins revealed that each one had a unique pattern of serine phosphorylation. Although there was one common site of phosphorylation, most likely located within the amino-terminal shared region, even this site showed quantitative differences in the level of phosphorylation for each of the proteins. Analysis of the Towne strain and two recent independent clinical isolates of human cytomegalovirus has shown that this family of proteins is highly conserved among human cytomegaloviruses.

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Section: Resultsmentioning

confidence: 99%

Posttranscriptional regulation of a class of human cytomegalovirus phosphoproteins encoded by an early transcription unit

Wright

Spector

1989

J Virol

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“…Although not established for HIV, in cells infected with a double-stranded DNA oncogenic adenovirus, the inhibition of the synthesis of cellular DNA and proteins, as well as the poly(ADP-ribosylation) of cellular histones, is followed by the extensive poly(ADP-ribosylation) of viral proteins (Goding et al, 1983) ; the ADPRT inhibitors, nicotinamide and benzamide, both depress viral yield up to 9-fold and viral infectivity up to 104-fold (Dery et al, 1986). Whereas these findings do not establish a direct effect on the poly(ADP-ribosylation) processing of viral proteins required for viral assembly and maturation, since other stages in the adenovirus cell cycle of infection may also be affected, they indicate that this would seem to be a stage which is also susceptible to the inhibition of ADPRT.…”

Section: )mentioning

confidence: 99%

New Directions for the Anti‐retroviral Chemotherapy of Aids ‐ a Basis for a Pharmacological Approach to Treatment

Alderson

1993

Biological Reviews

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At least 60 ADP-ribosylated variant histones are present in nuclei from dimethylsulfate-treated and untreated cells.

Boulikas

1988

The EMBO Journal

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The level of histone adenosine diphospho (ADP) ribosylation was studied in isolated nuclei from mouse myeloma cells in culture. The cells were treated with dimethylsulfate (DMS), a DNA‐methylating agent, and histones were analyzed using two‐dimensional gel electrophoresis. Seventeen or more bands probably representing mono‐to heptadeca (ADP‐ribosylated) histones could be visualized for each major variant histone. DMS treatment, by increasing the number of chromatin sites undergoing repair, greatly enhanced histone ADP‐ribosylation. When histones were labeled in a cell lysate rather than in isolated nuclei, mono‐ and oligo(ADP‐ribosylated) histone forms prevailed. The presence of approximately 87 ADP‐ribosylated variant histone forms in cell lysates and of approximately 170 in isolated nuclei is shown for the first time in this work. Previous studies show multiple ADP‐ribosylated forms for only histone H1. The theoretical number of variegated nucleosomes is thus much higher than previously thought, provided that histone‐histone contacts are not disrupted at up to a certain level of histone ADP‐ribosylation.

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ADP-ribosylation in in vitro Systems Synthesizing Adenovirus DNA

Cited by 10 publications

References 27 publications

Posttranscriptional regulation of a class of human cytomegalovirus phosphoproteins encoded by an early transcription unit

Posttranscriptional regulation of a class of human cytomegalovirus phosphoproteins encoded by an early transcription unit

New Directions for the Anti‐retroviral Chemotherapy of Aids ‐ a Basis for a Pharmacological Approach to Treatment

At least 60 ADP-ribosylated variant histones are present in nuclei from dimethylsulfate-treated and untreated cells.

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