Measles virus phosphoprotein (P) requires the NH2- and COOH-terminal domains for interactions with the nucleoprotein (N) but only the COOH terminus for interactions with itself.
A mammalian two-hybrid system was used to characterize protein-protein interactions between the measles virus nucleoprotein (N) and phosphoprotein (P). Progressive deletions at both the amino- and carboxy-termini of P facilitated the mapping of two distinct domains on P that are important for interaction with N: (i) a domain mapping predominantly within the C-terminal 100 amino acids and (ii) a domain composed of the extreme amino-terminal residues. Using the same two-hybrid assay, we discovered that the P protein interacts strongly with itself. In contrast to the N-P interaction, only a single C-proximal domain of P was essential for P-P interaction.
Harty
R N
RN
Department of Microbiology, Mount Sinai School of Medicine, New York, NY 10029-6574, USA.
Palese
P
P
D000596:Amino Acids / Q000032:analysis; D001665:Binding Sites; D002213:Capsid / Q000737:chemistry* / Q000378:metabolism; D008459:Measles virus / Q000737:chemistry*; D010750:Phosphoproteins; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D014758:Viral Core Proteins / Q000737:chemistry* / Q000378:metabolism; D014764:Viral Proteins / Q000737:chemistry* / Q000378:metabolism
D000596:Amino Acids; C055859:P protein, Sendai virus; D010750:Phosphoproteins; D011993:Recombinant Fusion Proteins; D014758:Viral Core Proteins; D014764:Viral Proteins