dc.contributor.author | Niskanen, Einari | |
dc.contributor.author | Kalliolinna, Olli | |
dc.contributor.author | Ihalainen, Teemu | |
dc.contributor.author | Häkkinen, Milla | |
dc.contributor.author | Vihinen-Ranta, Maija | |
dc.date.accessioned | 2016-01-29T09:17:08Z | |
dc.date.available | 2016-01-29T09:17:08Z | |
dc.date.issued | 2013 | |
dc.identifier.citation | Niskanen, 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.other | CONVID_22849709 | |
dc.identifier.other | TUTKAID_58014 | |
dc.identifier.uri | https://jyx.jyu.fi/handle/123456789/48522 | |
dc.description.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. 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.iso | eng | |
dc.relation.ispartofseries | Journal of Virology | |
dc.relation.uri | http://jvi.asm.org/ | |
dc.subject.other | parvovirus | |
dc.subject.other | NS1 proteiini | |
dc.subject.other | DNA:n sitoutuminen | |
dc.subject.other | NS1 protein | |
dc.subject.other | DNA binding | |
dc.title | Mutations in DNA Binding and Transactivation Domains Affect the Dynamics of Parvovirus NS1 Protein | |
dc.type | article | |
dc.identifier.urn | URN:NBN:fi:jyu-201601281311 | |
dc.contributor.laitos | Bio- ja ympäristötieteiden laitos | fi |
dc.contributor.laitos | Department of Biological and Environmental Science | en |
dc.contributor.oppiaine | Solu- ja molekyylibiologia | fi |
dc.contributor.oppiaine | Cell and Molecular Biology | en |
dc.type.uri | http://purl.org/eprint/type/JournalArticle | |
dc.date.updated | 2016-01-28T13:15:07Z | |
dc.type.coar | http://purl.org/coar/resource_type/c_2df8fbb1 | |
dc.description.reviewstatus | peerReviewed | |
dc.format.pagerange | 11762-11774 | |
dc.relation.issn | 0022-538X | |
dc.relation.numberinseries | 21 | |
dc.relation.volume | 87 | |
dc.type.version | publishedVersion | |
dc.rights.copyright | © 2013, American Society for Microbiology. Published in this repository with the kind permission of the publisher. | |
dc.rights.accesslevel | openAccess | fi |
dc.relation.doi | 10.1128/JVI.01678-13 | |
dc.type.okm | A1 | |