2013
Parvoviral Left-End Hairpin Ears Are Essential during Infection for Establishing a Functional Intranuclear Transcription Template and for Efficient Progeny Genome Encapsidation
Li L, Cotmore SF, Tattersall P. Parvoviral Left-End Hairpin Ears Are Essential during Infection for Establishing a Functional Intranuclear Transcription Template and for Efficient Progeny Genome Encapsidation. Journal Of Virology 2013, 87: 10501-10514. PMID: 23903839, PMCID: PMC3807388, DOI: 10.1128/jvi.01393-13.Peer-Reviewed Original ResearchConceptsDNA replicationA9 cellsC-terminal transactivation domainCapsid gene expressionProtein expressionWild-type virionsProgeny virion productionP38 promoterTransactivation domainTranscription complexInfectious plasmid cloneGenome encapsidationGenome packagingAbsence of progenyGene expressionPlasmid clonesTranscription templateMutant virionsNonstructural proteinsReplacement vectorViral transcriptionViral transcriptsSuch complementationVirion stabilityDuplex DNA
1998
Biochemical Activities of Minute Virus of Mice Nonstructural Protein NS1 Are Modulated In Vitro by the Phosphorylation State of the Polypeptide
Nüesch J, Corbau R, Tattersall P, Rommelaere J. Biochemical Activities of Minute Virus of Mice Nonstructural Protein NS1 Are Modulated In Vitro by the Phosphorylation State of the Polypeptide. Journal Of Virology 1998, 72: 8002-8012. PMID: 9733839, PMCID: PMC110136, DOI: 10.1128/jvi.72.10.8002-8012.1998.Peer-Reviewed Original ResearchConceptsHelicase activityBiochemical activityMultifunctional nuclear phosphoproteinEndogenous protein kinaseMajor nonstructural proteinIntrinsic helicase activityViral DNA replicationMinute virusCalf intestine alkaline phosphataseTarget DNA sequenceReplication extractThreonine residuesNonstructural protein NS1Particular phosphorylationInitiator proteinDNA replicationIntrinsic ATPasePosttranslational modificationsDNA motifsCellular promotersNuclear phosphoproteinProtein kinaseNickase activityDNA sequencesPhosphorylation state
1995
Sequence Motifs in the Replicator Protein of Parvovirus MVM Essential for Nicking and Covalent Attachment to the Viral Origin: Identification of the Linking Tyrosine
Nüesch J, Cotmore S, Tattersall P. Sequence Motifs in the Replicator Protein of Parvovirus MVM Essential for Nicking and Covalent Attachment to the Viral Origin: Identification of the Linking Tyrosine. Virology 1995, 209: 122-135. PMID: 7747462, DOI: 10.1006/viro.1995.1236.Peer-Reviewed Original ResearchConceptsMutant proteinsRolling-circle replicationTyrosine motifOrigin-containing plasmidParvoviral DNA replicationViral originParvovirus minute virusSingle-strand nicksInitiator proteinSequence motifsDNA replicationSite-specific bindingSequence comparisonCyanogen bromide cleavageOrigin sequencesDe novo synthesisSubstrate DNAY210Circle replicationLatter residueStrand nicksHeLa cellsLow salt conditionsCommon motifMetal coordination sites