The hypervariable C-terminal tail of the Sendai paramyxovirus nucleocapsid protein is required for template function but not for RNA encapsidation.
The paramyxovirus nucleocapsid proteins (NPs) are relatively well conserved, except for the C-terminal 20% (or ca. 100 amino acids), referred to as the tail. We have examined whether this hypervariable tail is required for genome synthesis, both in vitro, where synthesis is predominantly from the input templates, and in vivo, where multiple rounds of amplification occur. In these viruses, genome synthesis and assembly of the nascent chain are coupled. We find that the tail is required in vivo but not in vitro. Closer examination of the in vivo system showed that the tailless NP could encapsidate the genome chain but that amplification did not occur. We interpret these results as indicating that the tail is not required for RNA assembly but is required for the template to function in RNA synthesis. Relatively small deletions within the conserved N-terminal 80% of the protein, on the other hand, rendered the protein nonfunctional in either system. The possible functions of the tail in RNA synthesis are discussed.
Department of Genetics and Microbiology, University of Geneva School of Medicine, Switzerland.
J
J
Curran
H
H
Homann
C
C
Buchholz
S
S
Rochat
W
W
Neubert
D
D
Kolakofsky
D000595:Amino Acid Sequence; D002213:Capsid / Q000737:chemistry; D003001:Cloning, Molecular; D004252:DNA Mutational Analysis; D015967:Gene Expression Regulation, Viral; D066298:In Vitro Techniques; D008969:Molecular Sequence Data; D019590:Nucleocapsid Proteins; D009698:Nucleoproteins; D010222:Parainfluenza Virus 1, Human / Q000235:genetics*; D012367:RNA, Viral / Q000235:genetics*; D017384:Sequence Deletion; D013329:Structure-Activity Relationship; D014162:Transfection; D014758:Viral Core Proteins / Q000737:chemistry* / Q000235:genetics; D014779:Virus Replication
D019590:Nucleocapsid Proteins; D009698:Nucleoproteins; D012367:RNA, Viral; D014758:Viral Core Proteins