0000000000791070

AUTHOR

Milla M. Häkkinen

showing 2 related works from this author

Mutations in DNA Binding and Transactivation Domains Affect the Dynamics of Parvovirus NS1 Protein

2013

ABSTRACT The multifunctional replication protein of autonomous parvoviruses, NS1, is vital for viral genome replication and for the control of viral protein production. Two DNA-interacting domains of NS1, the N-terminal and helicase domains, are necessary for these functions. In addition, the N and C termini of NS1 are required for activation of viral promoter P38. By comparison with the structural and biochemical data from other parvoviruses, we identified potential DNA-interacting amino acid residues from canine parvovirus NS1. The role of the identified amino acids in NS1 binding dynamics was studied by mutagenesis, fluorescence recovery after photobleaching, and computer simulations. Mu…

HMG-boxParvovirus CaninevirusesImmunologyDNA Mutational AnalysisMutation MissenseNS1 proteiiniViral Nonstructural ProteinsVirus ReplicationMicrobiologyNS1 proteinSingle-stranded binding proteinCell LineSeqA protein domainVirologyAnimalsDNA bindingReplication protein AbiologyTer proteinparvovirusvirus diseasesDNAn sitoutuminen [DNA]biochemical phenomena metabolism and nutritionMolecular biologyCell biologyVirus-Cell InteractionsProtein Structure TertiaryDNA binding siteDNA-Binding ProteinsInsect Sciencebiology.proteinMutant ProteinsViral genome replicationBinding domainProtein Binding
researchProduct

Effect of ATP Binding and Hydrolysis on Dynamics of Canine Parvovirus NS1▿ †

2010

ABSTRACT The replication protein NS1 is essential for genome replication and protein production in parvoviral infection. Many of its functions, including recognition and site-specific nicking of the viral genome, helicase activity, and transactivation of the viral capsid promoter, are dependent on ATP. An ATP-binding pocket resides in the middle of the modular NS1 protein in a superfamily 3 helicase domain. Here we have identified key ATP-binding amino acid residues in canine parvovirus (CPV) NS1 protein and mutated amino acids from the conserved A motif (K406), B motif (E444 and E445), and positively charged region (R508 and R510). All mutations prevented the formation of infectious viruse…

Models MolecularParvovirus CaninevirusesImmunologyMolecular Sequence DataPlasma protein bindingViral Nonstructural ProteinsMicrobiologyCell Linechemistry.chemical_compoundAdenosine TriphosphateDogsVirologyAnimalsAmino Acid SequenceBinding siteBinding SitesbiologyHydrolysisDNA replicationHelicaseFluorescence recovery after photobleachingFusion proteinMolecular biologyGenome Replication and Regulation of Viral Gene ExpressionProtein Structure TertiaryViral replicationchemistryBiochemistryAmino Acid SubstitutionInsect Sciencebiology.proteinCatsMutagenesis Site-DirectedSequence AlignmentDNAProtein Binding
researchProduct