A potential nuclear envelope-targeting domain and an arginine-rich RNA binding element identified in the putative movement protein of the GAV strain of Barley yellow dwarf virus.

摘要

In this study, the structural elements in the putative movement protein (MP) of the GAV strain of Barley yellow dwarf virus (BYDV-GAV) were investigated. The GFP fusion protein of BYDV-GAV MP was found to be associated with the nuclear envelope (NE) in transgenic Arabidopsis thaliana (L.) cells. Serial deletion mapping demonstrated that the predicted alpha -helical domain located at the N-terminus of BYDV-GAV MP was required and sufficient for NE targeting in onion epidermal cells. This alpha -helical domain does not contain any sequence elements similar to known nuclear localisation signals or bear any significant resemblance to previously characterised NE-targeting structure, indicating that it may represent a novel NE-targeting domain in plant cells. Deletion mutagenesis showed that the C-terminal end of BYDV-GAV MP possessed an element required for its RNA binding activity in vitro. Further analysis revealed that the arginine amino acids within the last 11 residues of the C-terminal end were crucial for the binding of BYDV-GAV MP to RNA. This C-terminal element enriched in basic residues was also present in the MPs of other BYDV strains and the polerovirus Potato leaf roll virus (PLRV), suggesting the conservation of a RNA binding element in the MPs from both luteoviruses and poleroviruses. The data in this work present an initial characterisation of a novel plant NE-targeting domain and a RNA binding element on BYDV-GAV MP. Further studies are underway to investigate the function of these elements in the biology of natural BYDV-GAV infection.