Mutations in conserved domain I of the Sendai virus L polymerase protein uncouple transcription and replication.

@article{Chandrika1995MutationsIC,
  title={Mutations in conserved domain I of the Sendai virus L polymerase protein uncouple transcription and replication.},
  author={R. Chandrika and S M Horikami and Sherin E. Smallwood and Sue A. Moyer},
  journal={Virology},
  year={1995},
  volume={213 2},
  pages={352-63}
}
To begin to map functional domains of the Sendai P-L RNA polymerase complex we wanted to characterize the P binding site on the Sendai L protein. Analysis of in vitro and in vivo P-L polymerase complex formation with carboxyl-truncations of the L protein showed that the N-terminal half of the protein was required. Site-directed mutagenesis of the Sendai virus L gene was employed to change amino acids within a highly conserved region of the N-terminal domain I from amino acids (aa) 348-379… CONTINUE READING

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