title: Neither phosphorylation nor the amino-terminal part of rabies virus phosphoprotein is required for its oligomerization.
abstract: 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.
authors.affiliation: Laboratoire d'Enzymologie et Biochimie Structurales (LEBS), CNRS, 91198 Gif sur Yvette, France.
authors.forename: B
authors.initials: B
authors.lastname: Gigant
authors.forename: F
authors.initials: F
authors.lastname: Iseni
authors.forename: Y
authors.initials: Y
authors.lastname: Gaudin
authors.forename: M
authors.initials: M
authors.lastname: Knossow
authors.forename: D
authors.initials: D
authors.lastname: Blondel
mesh_terms: 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
chemical_list: D018832:Molecular Chaperones; C103961:P phosphoprotein, Rabies virus; D010750:Phosphoproteins; D015678:Viral Structural Proteins