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dc.contributor.authorNiskanen, Einari
dc.contributor.authorKalliolinna, Olli
dc.contributor.authorIhalainen, Teemu
dc.contributor.authorHäkkinen, Milla
dc.contributor.authorVihinen-Ranta, Maija
dc.date.accessioned2016-01-29T09:17:08Z
dc.date.available2016-01-29T09:17:08Z
dc.date.issued2013
dc.identifier.citationNiskanen, E., Kalliolinna, O., Ihalainen, T., Häkkinen, M., & Vihinen-Ranta, M. (2013). Mutations in DNA Binding and Transactivation Domains Affect the Dynamics of Parvovirus NS1 Protein. <i>Journal of Virology</i>, <i>87</i>(21), 11762-11774. <a href="https://doi.org/10.1128/JVI.01678-13" target="_blank">https://doi.org/10.1128/JVI.01678-13</a>
dc.identifier.otherCONVID_22849709
dc.identifier.otherTUTKAID_58014
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/48522
dc.description.abstractThe 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. Mutations in the predicted DNA-interacting amino acids of the N-terminal and helicase domains increased the intranuclear binding dynamics of NS1 dramatically. A substantial increase in binding dynamics was also observed for NS1 mutants that targeted the metal ion coordination site in the N terminus. Interestingly, contrary to other mutants, deletion of the C terminus resulted in slower binding dynamics of NS1. P38 transactivation was severely reduced in both N-terminal DNA recognition and in C-terminal deletion mutants. These data suggest that the intranuclear dynamics of NS1 are largely characterized by its sequence-specific and -nonspecific binding to double-stranded DNA. Moreover, binding of NS1 is equally dependent on the N-terminal domain and conserved -loop of the helicase domain.
dc.language.isoeng
dc.relation.ispartofseriesJournal of Virology
dc.relation.urihttp://jvi.asm.org/
dc.subject.otherparvovirus
dc.subject.otherNS1 proteiini
dc.subject.otherDNA:n sitoutuminen
dc.subject.otherNS1 protein
dc.subject.otherDNA binding
dc.titleMutations in DNA Binding and Transactivation Domains Affect the Dynamics of Parvovirus NS1 Protein
dc.typearticle
dc.identifier.urnURN:NBN:fi:jyu-201601281311
dc.contributor.laitosBio- ja ympäristötieteiden laitosfi
dc.contributor.laitosDepartment of Biological and Environmental Scienceen
dc.contributor.oppiaineSolu- ja molekyylibiologiafi
dc.contributor.oppiaineCell and Molecular Biologyen
dc.type.urihttp://purl.org/eprint/type/JournalArticle
dc.date.updated2016-01-28T13:15:07Z
dc.type.coarjournal article
dc.description.reviewstatuspeerReviewed
dc.format.pagerange11762-11774
dc.relation.issn0022-538X
dc.relation.numberinseries21
dc.relation.volume87
dc.type.versionpublishedVersion
dc.rights.copyright© 2013, American Society for Microbiology. Published in this repository with the kind permission of the publisher.
dc.rights.accesslevelopenAccessfi
dc.relation.doi10.1128/JVI.01678-13


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