The movement protein of barley yellow dwarf virus-GAV self-interacts and forms homodimers in vitro and in vivo

The movement protein of barley yellow dwarf virus-GAV self-interacts and forms homodimers in... 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Virology Springer Journals

The movement protein of barley yellow dwarf virus-GAV self-interacts and forms homodimers in vitro and in vivo

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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
D.O.I.
10.1007/s00705-012-1288-9
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 VirologySpringer Journals

Published: Jul 1, 2012

References

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