AltMV TGB1 Nucleolar Localization Requires Homologous Interaction and Correlates with Cell Wall Localization Associated with Cell-to-Cell Movement

다국어 초록 (Multilingual Abstract)

The Potexvirus Alternanthera mosaic virus (AltMV) hasmultifunctional triple gene block (TGB) proteins, amongwhich our studies have focused on the properties of theTGB1 protein. The TGB1 of AltMV has functionsincluding RNA binding, RNA silencing suppression,and cell-to-cell movement, and is known to form homologousinteractions. The helicase domains of AltMVTGB1 were separately mutated to identify which regionsare involved in homologous TGB1 interactions. Theyeast two hybrid system and Bimolecular FluorescenceComplementation (BiFC) in planta were utilized to examinehomologous interactions of the mutants. Helicasemotif I of AltMV TGB1 was found to be critical tomaintain homologous interactions. Mutations in theremaining helicase motifs did not inhibit TGB1 homologousinteractions. In the absence of homologous interactionof TGB1, subcellular localization of helicasedomain I mutants showed distinctively different patternsfrom that of WT TGB1. These results provide importantinformation to study viral movement and replicationof AltMV.

참고문헌 (Reference)

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