Deletion Analysis Defines a Carboxyl-Proximal Region of Sendai Virus P Protein That Binds to the Polymerase L Protein

作者: Sherin Smallwood , Kevin W. Ryan , Sue A. Moyer

DOI: 10.1006/VIRO.1994.1331

关键词: Amino acidMolecular biologyNuclear cap-binding protein complexProtein GProtein A/GBiologySendai virusHSPA2RNA polymerase complexBinding siteVirology

摘要: The Sendai virus RNA polymerase complex consists of two viral proteins, L and P, which must be coexpressed in order to form the active enzyme. Pulse-chase experiments show that protein is unstable when synthesized absence P protein, but stable P-L complex. Using sequential deletions (568 amino acids), we have mapped site on where binds by co-immunoprecipitation gradient sedimentation analyses. L-binding residues C-terminal half since deletion up acid 324 does not affect formation. was a region encompassing acids 412-478. This lies between previously regions nucleocapsid-binding domain (amino 345-411 479-568). data suggest NP protein-binding domains do overlap.

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