Cell-to-cell progression of tobacco mosaic virus (TMV) infection in plants
depends on virus-encoded movement protein (MP). Here we show that a conserv
ed sequence motif in tobamovirus MPs shares similarity with a region in tub
ulins that is proposed to mediate lateral contacts between microtubule prot
ofilaments. Point mutations in this motif confer temperature sensitivity to
microtubule association and viral-RNA intercellular-transport functions of
the protein, indicating that MP-interacting microtubules are functionally
involved in the transport of vRNA to plasmodesmata. Moreover, we show that
MP interacts with microtubule-nucleation sites. Together, our results indic
ate that MP may mimic tubulin assembly surfaces to propel vRNA transport by
a dynamic process that is driven by microtubule polymerization.