Minute Virus of Mice Non-structural Protein NS-1 Is Necessary and Sufficient for Trans-activation of the Viral P39 Promoter

Doerig, Christian; Hirt, Bernhard; Beard, Peter; Antonietti, Jean‐Philippe

doi:10.1099/0022-1317-69-10-2563

Cited by 100 publications

(85 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…When the mutant plasmid (p385UTT) was transfected into murine A9 fibroblasts, very little P38-generated R3 RNA was detected, as expected (Fig. 2, lane 8), because the P38 promoter is dependent on NS1 for activation (Rhode 1985;Doerig et al 1988;Schoborg and Pintel 1991). In addition, a significantly higher ratio of accumulated R1 to R2 was seen compared with parallel transfections of wild-type plasmids ( Fig.…”

Section: Artificially Introduced Ochre Termination Codons In the Nonsmentioning

confidence: 68%

Nonsense mutations inhibit splicing of MVM RNA in cis when they interrupt the reading frame of either exon of the final spliced product.

Naeger

Schoborg²,

Zhao³

et al. 1992

Genes Dev.

129

146

View full text Add to dashboard Cite

Missouri 65212 USA mRNAs R1 and R2 of the autonomous parvovirus minute virus of mice (MVM), which encode the viral nonstructural proteins NS1 and NS2, respectively, are processed in an ordered splicing pathway in which R2 is generated from mature spliced R1. Introduction of translation termination signals into these genes alters the processing of these RNAs; there is a significant (up to fourfold) increase in the accumulated steady-state levels of R1 relative to R2, when compared with wild-type levels, although the total accumulated levels of R1 plus R2 remain the same. The increase in accumulated R1 relative to R2 in mutant infected or transfected murine cells is independent of RNA stability and transport and decreases, in a polar manner, with the distance of the inserted termination signal from the shared initiation codon for NS1 and NS2 at nucleotide 260. The increased ratio of R1 to R2 is a consequence of the artificially introduced translation termination signals acting in cis rather than in the absence of a functional viral gene product. These mutations have an effect when they interrupt previously open reading frames in either exon of the spliced product R2. Nonsense mutations that are located in the second exon of R2 inhibit splicing of R1 to R2 only when they interrupt an open reading frame (ORF) that has the potential, after normal splicing, to be joined in-frame with the initiating AUG. These results suggest that nonsense mutations inhibit splicing of R1 to R2 by influencing the mechanism by which exons are defined in murine cells.

show abstract

Section: Artificially Introduced Ochre Termination Codons In the Nonsmentioning

confidence: 68%

Nonsense mutations inhibit splicing of MVM RNA in cis when they interrupt the reading frame of either exon of the final spliced product.

Naeger

Schoborg²,

Zhao³

et al. 1992

Genes Dev.

129

146

View full text Add to dashboard Cite

show abstract

“…1B), and single-stranded genomes resulting from the encapsidation of replicative forms into maturing virions (17) were synthesized to high levels in these cells as well. The expression of the nonstructural protein NS-1, a cytotoxic polypeptide (11,41) essential for replication and packaging of parvovirus DNA (11,14,16) and for transactivation of the viral promoters (18,19,51), was monitored by a fluorescence-activated cell sorting-based procedure with an NS-1-specific MAb. In the example shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

Parvovirus Infection Suppresses Long-Term Repopulating Hematopoietic Stem Cells

Segovia

Güenechea

Gallego

et al. 2003

J Virol

View full text Add to dashboard Cite

“…The genome of autonomous parvoviruses comprises two transcription units, encoding the nonstructural proteins NS1 and NS2 and the capsid proteins VP1 and VP2 (231). NS1 is a multifunctional phosphoprotein that acts as a transcriptional activator of viral promoters as well as initiator and helicase in parvoviral DNA replication (232)(233)(234)(235)(236)(237). Furthermore, NS1 colocalizes with replicating viral DNA in virus-induced nuclear foci (238,239).…”

Section: Nuclear Dna Virus Replication Centersmentioning

confidence: 99%

DNA Virus Replication Compartments

Schmid

Speiseder

Dobner

et al. 2014

J Virol

146

142

View full text Add to dashboard Cite

bViruses employ a variety of strategies to usurp and control cellular activities through the orchestrated recruitment of macromolecules to specific cytoplasmic or nuclear compartments. Formation of such specialized virus-induced cellular microenvironments, which have been termed viroplasms, virus factories, or virus replication centers, complexes, or compartments, depends on molecular interactions between viral and cellular factors that participate in viral genome expression and replication and are in some cases associated with sites of virion assembly. These virus-induced compartments function not only to recruit and concentrate factors required for essential steps of the viral replication cycle but also to control the cellular mechanisms of antiviral defense. In this review, we summarize characteristic features of viral replication compartments from different virus families and discuss similarities in the viral and cellular activities that are associated with their assembly and the functions they facilitate for viral replication.

show abstract

Minute Virus of Mice Non-structural Protein NS-1 Is Necessary and Sufficient for Trans-activation of the Viral P39 Promoter

Cited by 100 publications

References 34 publications

Nonsense mutations inhibit splicing of MVM RNA in cis when they interrupt the reading frame of either exon of the final spliced product.

Nonsense mutations inhibit splicing of MVM RNA in cis when they interrupt the reading frame of either exon of the final spliced product.

Parvovirus Infection Suppresses Long-Term Repopulating Hematopoietic Stem Cells

DNA Virus Replication Compartments

Contact Info

Product

Resources

About