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- Publisher
- Springer Journals
- Copyright
- Copyright © 2012 by Springer-Verlag
- Subject
- Biomedicine; Infectious Diseases; Medical Microbiology; Virology
- ISSN
- 0304-8608
- eISSN
- 1432-8798
- DOI
- 10.1007/s00705-012-1288-9
- pmid
- 22437255
- Publisher site
- See Article on Publisher Site
Abstract
The 17-kDa movement protein (MP) of the GAV strain of barley yellow dwarf virus (BYDV-GAV) can bind the viral RNA and target to the nucleus. However, much less is known about the active form of the MP in planta . In this study, the ability of the MP to self-interact was analyzed by yeast two-hybrid assay and bimolecular fluorescence complementation. The BYDV-GAV MP has a strong potential to self-interact in vitro and in vivo , and self-interaction was mediated by the N-terminal domain spanning the second α-helix (residues 17-39). Chemical cross-linking and heterologous MP expression from a pea early browning virus (PEBV) vector further showed that MP self-interacts to form homodimers in vitro and in planta . Interestingly, the N-terminal domain necessary for MP self-interaction has previously been identified as important for nuclear targeting. Based on these findings, a functional link between MP self-interaction and nuclear targeting is discussed.
Journal
Archives of Virology – Springer Journals
Published: Jul 1, 2012