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Journal of Biochemistry Advance Access published online on January 3, 2009
Journal of Biochemistry, doi:10.1093/jb/mvn180
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© The authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.

Turnip mosaic virus genome-linked protein VPg binds C-terminal region of cap-bound initiation factor 4E ortholog without exhibiting host cellular specificity

Hayato Okade1, Yuki Fujita1, Saori Miyamoto1, Koji Tomoo1,{dagger}, Shinji Muto2, Hiroshi Miyoshi2, Tomohide Natsuaki3, Robert E. Rhoads4 and Toshimasa Ishida1

1Department of Physical Chemistry, Osaka University of Pharmaceutical Sciences, 4-20-1 Nasahara, Takatsuki, Osaka 569-1094, Japan; 2Department of Microbiology, St. Marianna University School of Medicine, Kawasaki 216-8511, Japan; 3Genomic Research Institute and Faculty of Agriculture, Utsunomiya University, Utsunomiya 321-8505, Japan; and 4Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, Shreveport, Louisiana 71130, USA

{dagger}To whom correspondence should be addressed: Koji Tomoo: email: tomoo{at}gly.oups.ac.jp

Received October 10, 2008; Accepted November 26, 2008


  Abstract

To investigate the binding specificity of turnip mosaic virus (TuMV) VPg (Viral Protein-genome linked) with translation initiation factor 4E, we evaluated here the kinetic parameters for the interactions of human eIF4E, C.elegans IFE-3 and IFE-5, and Arabidopsis eIFiso4E, by surface plasmon resonance (SPR). The results indicated that TuMV VPg does not show a binding preference for Arabidopsis eIFiso4E, even though it is from a host species whereas the other eIF4E orthologs are not. Surprisingly, the effect of m7GTP on both the rate constants and equilibrium binding constants for the interactions of VPg differed for the four eIF4E orthologs. In the case of eIFiso4E and IFE-3, m7GTP increased kon, but for eIF4E and IFE-5, it decreased kon. To provide insight into the structural basis for these differences in VPg binding, tertiary structures of the eIF4E orthologs were predicted on the basis of the previously determined crystal structure of m7GpppA-bound human eIF4E. The results suggested that in cap-bound eIF4E orthologs, the VPg binds to the C-terminal region, which constitutes one side of the entrance to the cap-binding pocket, whereas in the cap-free state, VPg binds to the widely opened cap-binding pocket and its surrounding region. The binding of VPg to the C-terminal region was confirmed by the SPR analyses of N- or C-terminal residues-deleted eIF4E orthologs.

Key Words: turnip mosaic virus, VPg, eIF4E, surface plasmon resonance, 3D structure prediction


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