2014
Complementation for an essential ancillary non-structural protein function across parvovirus genera
Mihaylov IS, Cotmore SF, Tattersall P. Complementation for an essential ancillary non-structural protein function across parvovirus genera. Virology 2014, 468: 226-237. PMID: 25194919, PMCID: PMC4254310, DOI: 10.1016/j.virol.2014.07.043.Peer-Reviewed Original ResearchConceptsCell cycle progressionAncillary proteinsProtein functionDNA replicationReplication centersNP1 proteinPrimary sequenceFunctional overlapProtein NS2Cycle progressionGenus BocaparvovirusGenus ProtoparvovirusLate defectsNP1 inductionParvovirus genusVirion productionMinute virusSpecific defectsCell populationsUninfected cellsGenusCell viabilityProteinHuman bocavirus 1NP1 expression
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
2010
Recruitment of DNA replication and damage response proteins to viral replication centers during infection with NS2 mutants of Minute Virus of Mice (MVM)
Ruiz Z, Mihaylov IS, Cotmore SF, Tattersall P. Recruitment of DNA replication and damage response proteins to viral replication centers during infection with NS2 mutants of Minute Virus of Mice (MVM). Virology 2010, 410: 375-384. PMID: 21193212, PMCID: PMC3072075, DOI: 10.1016/j.virol.2010.12.009.Peer-Reviewed Original ResearchConceptsViral replication centersDamage responseReplication centersDamage response proteinsMutant infectionDNA damage responsePhosphorylation of ATRNS2 mutantsProtein recruitmentViral DNA amplificationATM activationCellular proteinsDNA replicationReplication factorsResponse proteinsBody maturationA9 cellsMVM infectionMinute virusWidespread associationWestern transferDNA amplificationMechanism of actionProteinRecruitment
2008
Parvoviruses: General Features
Tattersall P. Parvoviruses: General Features. 2008, 90-97. DOI: 10.1016/b978-012374410-4.00463-5.Peer-Reviewed Original ResearchDNA replication initiator proteinParvovirus DNA replicationReplication initiator proteinSubfamily DensovirinaeArthropod speciesInitiator proteinDNA replicationSubfamily ParvovirinaeDNA genomeCoding sequenceGenetic strategiesNonenveloped virusesGenomic moleculesVertebrate hostsExpression cassetteTerminal repeatFamily ParvoviridaeGenusTerminal hairpinsStructural polypeptidesDensovirinaeSequenceGenomeInsectsTelomeres
2001
A consensus DNA recognition motif for two KDWK transcription factors identifies flexible-length, CpG-methylation sensitive cognate binding sites in the majority of human promoters11Edited by M. Yaniv
Burnett E, Christensen J, Tattersall P. A consensus DNA recognition motif for two KDWK transcription factors identifies flexible-length, CpG-methylation sensitive cognate binding sites in the majority of human promoters11Edited by M. Yaniv. Journal Of Molecular Biology 2001, 314: 1029-1039. PMID: 11743720, DOI: 10.1006/jmbi.2000.5198.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsBase SequenceBinding SitesConsensus SequenceCpG IslandsDimerizationDNADNA MethylationDNA-Binding ProteinsElectrophoretic Mobility Shift AssayHeLa CellsHumansKineticsMolecular WeightPromoter Regions, GeneticProtein BindingProtein SubunitsResponse ElementsSubstrate SpecificityTranscription FactorsConceptsParvovirus initiation factorTranscription factorsDNA recognition motifDNA-binding heterodimersParvoviral DNA replicationTranscriptional start siteCellular transcription factorsEukaryotic genomesProtein complexesDNA replicationM. YanivInitiation factorsStart siteCpG methylationHuman promotersRecognition motifCytosine residuesRecombinant baculovirusSelection experimentsElement upstreamC residuesHeLa cellsPromoterHeterodimersHost factors
1999
Two New Members of the Emerging KDWK Family of Combinatorial Transcription Modulators Bind as a Heterodimer to Flexibly Spaced PuCGPy Half-Sites
Christensen J, Cotmore S, Tattersall P. Two New Members of the Emerging KDWK Family of Combinatorial Transcription Modulators Bind as a Heterodimer to Flexibly Spaced PuCGPy Half-Sites. Molecular And Cellular Biology 1999, 19: 7741-7750. PMID: 10523663, PMCID: PMC84824, DOI: 10.1128/mcb.19.11.7741.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceBinding SitesCloning, MolecularDimerizationDNA-Binding ProteinsDNA, ComplementaryGC Rich SequenceHeLa CellsHumansMolecular Sequence DataMultigene FamilyNuclear ProteinsParvovirusPromoter Regions, GeneticProtein BindingReceptors, TransferrinRecombinant ProteinsReplication OriginSequence Homology, Amino AcidTranscription FactorsTyrosine TransaminaseConceptsParvovirus initiation factorPromoter activation assaysParvovirus DNA replicationE-box motifAmino acid identityTransferrin receptor promoterResponse element-binding proteinCyclic AMP response element binding proteinElement-binding proteinHeLa factorsAMP response element binding proteinTranscriptional modulatorDNA replicationHuman cDNAAcid identityInitiation factorsRegulatory elementsDEAF-1Recombinant baculovirusHalf sitesPromoter regionComplex bindsReceptor promoterHost cellsComplex consisting
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
1997
Parvovirus initiation factor PIF: a novel human DNA-binding factor which coordinately recognizes two ACGT motifs
Christensen J, Cotmore S, Tattersall P. Parvovirus initiation factor PIF: a novel human DNA-binding factor which coordinately recognizes two ACGT motifs. Journal Of Virology 1997, 71: 5733-5741. PMID: 9223459, PMCID: PMC191825, DOI: 10.1128/jvi.71.8.5733-5741.1997.Peer-Reviewed Original ResearchConceptsDNA-binding factorsACGT motifGel mobility shift assaysReplication initiation processMobility shift assaysHigher-order multimersParvovirus initiation factorSame cellular factorHeLa S3 cellsMouse genomeBinds DNADNA replicationACGT sequenceInitiation factorsOrigin sequencesShift assaysMinimal originMutant oligonucleotidesATP hydrolysisMobility shiftDNase ICellular factorsEssential cofactorMobility assaysSingle binding siteA novel cellular site-specific DNA-binding protein cooperates with the viral NS1 polypeptide to initiate parvovirus DNA replication
Christensen J, Cotmore S, Tattersall P. A novel cellular site-specific DNA-binding protein cooperates with the viral NS1 polypeptide to initiate parvovirus DNA replication. Journal Of Virology 1997, 71: 1405-1416. PMID: 8995666, PMCID: PMC191197, DOI: 10.1128/jvi.71.2.1405-1416.1997.Peer-Reviewed Original ResearchConceptsReplication protein AProliferating-cell nuclear antigenOrigin replicationDNA replicationSite-specific DNA-binding proteinRecombinant replication protein AUV cross-linking analysisParvovirus DNA replicationDNA-binding proteinsSequence-specific DNACross-linking analysisSimian virus 40 replicationParvovirus initiation factorCellular proteinsInitiation factorsTranscription factorsEndonuclease functionMinimal originGel shiftMVM replicationNS1 polypeptideSpecific nickingS100 extractsSite regionDNA proceeds
1995
DNA replication in the autonomous parvoviruses
Cotmore S, Tattersall* P. DNA replication in the autonomous parvoviruses. Seminars In Virology 1995, 6: 271-281. DOI: 10.1006/smvy.1995.0033.Peer-Reviewed Original ResearchShort palindromic sequencesSpecific origin sequencesUnit-length genomesDNA synthesisViral NS1 proteinProgeny DNA synthesisLeading-strand synthesisSingle-strand nicksDNA replicationDNA genomeOrigin sequencesPalindromic sequenceAutonomous parvovirusesGenomeNew copiesNS1 proteinTelomeresReplicationOngoing replicationSequence 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
1989
Limitations to the expression of parvoviral nonstructural proteins may determine the extent of sensitization of EJ-ras-transformed rat cells to minute virus of mice
Van Hille B, Duponchel N, Salomé N, Spruyt N, Cotmore S, Tattersall P, Cornelis J, Rommelaere J. Limitations to the expression of parvoviral nonstructural proteins may determine the extent of sensitization of EJ-ras-transformed rat cells to minute virus of mice. Virology 1989, 171: 89-97. PMID: 2525841, DOI: 10.1016/0042-6822(89)90514-x.Peer-Reviewed Original ResearchConceptsNonstructural proteinsNonstructural protein NS-1Parvoviral DNA replicationRat cellsParvoviral life cycleNonstructural viral proteinsDNA replicationRat cell linesSensitivity of cellsRas transformationP21ras proteinsNormal rat cellsGene expressionMVMp infectionParvovirus MVMpNRK cellsViral proteinsEarly blockProteinCell linesViral DNALife cycleNS-1MVMpExpressionEvidence for a ligation step in the DNA replication of the autonomous parvovirus minute virus of mice
Cotmore S, Gunther M, Tattersall P. Evidence for a ligation step in the DNA replication of the autonomous parvovirus minute virus of mice. Journal Of Virology 1989, 63: 1002-1006. PMID: 2911112, PMCID: PMC247784, DOI: 10.1128/jvi.63.2.1002-1006.1989.Peer-Reviewed Original Research