Neither phosphorylation nor the amino-terminal part of rabies virus phosphoprotein is required for its oligomerization.
Rabies virus (PV strain) phosphoprotein (P) was expressed in bacteria. This recombinant protein binds specifically to the nucleoprotein-RNA complex purified from infected cells. Chemical cross-linking and gel-filtration studies indicated that the P protein forms oligomers. Analytical centrifugation data demonstrated the co-existence of monomeric and oligomeric forms of rabies virus P protein and suggested that there is an equilibrium between these species. As P expressed in bacteria is not phosphorylated, this result indicates that P phosphorylation is not required for its oligomerization. Although an alignment of several rhabdovirus P sequences revealed that the amino-terminal domain of P has a conserved predicted propensity to form helical coiled coils, an amino-terminally truncated form of P protein, lacking the first 52 residues, was also shown to be oligomeric. Therefore, the amino-terminal domain of rabies virus P is not necessary for its oligomerization.
Gigant
B
B
Laboratoire d'Enzymologie et Biochimie Structurales (LEBS), CNRS, 91198 Gif sur Yvette, France.
Iseni
F
F
Gaudin
Y
Y
Knossow
M
M
Blondel
D
D
D000595:Amino Acid Sequence; D018832:Molecular Chaperones; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010750:Phosphoproteins / Q000737:chemistry* / Q000502:physiology; D010766:Phosphorylation; D015678:Viral Structural Proteins / Q000737:chemistry* / Q000502:physiology
D018832:Molecular Chaperones; C103961:P phosphoprotein, Rabies virus; D010750:Phosphoproteins; D015678:Viral Structural Proteins