Mutations in DNA binding and transactivation domains affect the dynamics of parvovirus NS1 protein.

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 intr

SUBMITTER: Niskanen EA 

PROVIDER: S-EPMC3807334 | biostudies-literature | 2013 Nov

REPOSITORIES: biostudies-literature