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Virology. 1994 Jul;202(1):154-63.

Deletion analysis defines a carboxyl-proximal region of Sendai virus P protein that binds to the polymerase L protein.

Author information

1
Department of Immunology and Medical Microbiology, College of Medicine, University of Florida, Gainesville 32610-0266.

Abstract

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

PMID:
8009828
DOI:
10.1006/viro.1994.1331
[Indexed for MEDLINE]

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