Interaction between the movement protein of barley yellow dwarf virus and the cell nuclear envelope: Role of a putative amphiphilic α-helix at the N-terminus of the movement protein

Biopolymers ◽  
2005 ◽  
Vol 79 (2) ◽  
pp. 86-96 ◽  
Author(s):  
Kunfan Liu ◽  
Zongliang Xia ◽  
Yan Zhang ◽  
Yuxiang Wen ◽  
Daowen Wang ◽  
...  
Keyword(s):  
Nuclear Envelope ◽  
Barley Yellow Dwarf Virus ◽  
Movement Protein ◽  
Yellow Dwarf ◽  
Dwarf Virus ◽  
Barley Yellow Dwarf ◽  
N Terminus ◽  
Yellow Dwarf Virus ◽  
Α Helix

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

2008 ◽  
Vol 35 (1) ◽  
pp. 40 ◽  
Author(s):  
Zongliang Xia ◽  
Yan Wang ◽  
Zhiqiang Du ◽  
Junmin Li ◽  
Richard Y. Zhao ◽  
...  
Keyword(s):  
Nuclear Envelope ◽  
Rna Binding ◽  
Barley Yellow Dwarf Virus ◽  
Movement Protein ◽  
Yellow Dwarf ◽  
Dwarf Virus ◽  
Helical Domain ◽  
Barley Yellow Dwarf ◽  
Putative Movement Protein ◽  
Yellow Dwarf Virus

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 α-helical domain located at the N-terminus of BYDV-GAV MP was required and sufficient for NE targeting in onion epidermal cells. This α-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.

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