The Measles Virus Nucleocapsid Protein Tail Domain Is Dispensable for Viral Polymerase Recruitment and Activity

• Published in: The Journal of biological chemistry Vol. 288; no. 41; pp. 29943 - 29953
• Main Authors: Krumm, Stefanie A., Takeda, Makoto, Plemper, Richard K.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 11.10.2013; American Society for Biochemistry and Molecular Biology
• Subjects: Animal Viruses; Animals; Binding Sites - genetics; Cell Line; Chlorocebus aethiops; Immunoblotting; Measles virus - genetics; Measles virus - metabolism; Microbiology; Models, Molecular; Mutation; Nucleocapsid Proteins; Nucleoproteins - chemistry; Nucleoproteins - genetics; Nucleoproteins - metabolism; Protein Binding; Protein Structure, Tertiary; Protein Subunits - chemistry; Protein Subunits - genetics; Protein Subunits - metabolism; Ribonucleoproteins - chemistry; Ribonucleoproteins - genetics; Ribonucleoproteins - metabolism; RNA-Dependent RNA Polymerase - chemistry; RNA-Dependent RNA Polymerase - genetics; RNA-Dependent RNA Polymerase - metabolism; Vero Cells; Viral Polymerase; Viral Proteins - chemistry; Viral Proteins - genetics; Viral Proteins - metabolism; Viral Replication; Virus; Virus Replication; Virus; Viral Replication; Animal Viruses; Microbiology; Viral Polymerase

Paramyxovirus genomes are ribonucleoprotein (RNP) complexes consisting of nucleoprotein (N)-encapsidated viral RNA. Measles virus (MeV) N features an amino-terminal RNA-binding core and a 125-residue tail domain, of which only the last 75 residues are considered fully mobile on the nucleocapsid surf...