The Phosphorylation of NS Protein of Wheat Rosette Stunt
Virus

XIE Bao-Tong, YE
Yong-Jun, GONG Zu-Xun*

( Key
Laboratory of Proteomics, Institute of Biochemistry and Cell Biology, Shanghai
Institutes for Biological Sciences, the Chinese Academy of Sciences, Shanghai
200031, China )

Abstract        The
genome of wheat rosette stunt virus (WRSV), a plant rhabdovirus, is a single
negative strand RNA. It encodes five viral structural proteins: the
glycoprotein (G), the matrix protein (M), the nucleocapsid protein (N), the
large protein (L) and the non-structural protein (NS), which was later proved
to be a viral structural protein too and existed in a variety of
phosphorylation forms in case of vascular stomatitis virus (VSV). In this paper
we demonstrated that NS protein of WRSV, either bound with the viral
nucleocapsid or expressed in bacteria could be in vitro phosphorylated
in presence of viral nucleocapsid. We concluded that the NS protein of WRSV was
a phosphorylated protein and it might exist in both phosphorylated and
dephosphorylated forms in virions. Our results excluded the possibility that
the NS protein could be autophosphorylated. The L protein, the major component
of viral RNA dependent RNA polymerase is associated with the protein kinase for
phosphorylation of NS protein.

Key words     wheat
rosette stunt virus; NS protein; phosphorylation; protein kinase

*Corresponding
author: Tel, 86-21-54921220; Fax, 86-21-54921125;
e-mail, [email protected]