The ability of the matrix (M) protein of potato yellow dwarf virus (PYDV) to remodel nuclear membranes is controlled by a dileucine motif located at residues 223 and 224 of its primary structure. This function can be uncoupled from that of its nuclear localization signal (NLS), which is controlled primarily by lysine and arginine residues immediately downstream of the LL motif. In planta localization of green fluorescent protein fusions, bimolecular fluorescence complementation assays with nuclear import receptor importin-a1 and yeast-based nuclear import assays provided three independent experimental approaches to validate the authenticity of the M-NLS. The carboxy terminus of M is predicted to contain a nuclear export signal, which is belived to be functional, given the ability of M to bind the Arabidopsis nuclear export receptor 1 (XPO1). The nuclear shuttle activity of M has implications for the cell-to-cell movement of PYDV nucleocapsids, based upon its interaction with the N and Y proteins.
|Number of pages||10|
|Journal||Journal of General Virology|
|State||Published - May 2018|
Bibliographical noteFunding Information:
This research was supported, in part, by grant 0749519 from the US National Science Foundation and grant KSEF-3490-RDE-019 from the Kentucky Science and Engineering Foundation awarded to M.G.
© 2018, Microbiology Society. All rights reserved.
- Inner nuclear membrane
- Nicotiana benthamiana
- Nuclear export
- Nuclear import
ASJC Scopus subject areas