AI Article Synopsis
- The 32-kDa movement protein P3 from alfalfa mosaic virus is crucial for the virus's movement between plant cells.
- In tests with Nicotiana tabacum, P3 mainly appeared in cell walls of older leaves and in the cytosol of younger ones, while in Pichia pastoris, it was found primarily in a soluble state.
- Metabolic labeling showed that P3 underwent phosphorylation in both organisms, indicating that this modification likely influences its function like in other viral movement proteins.
Article Abstract
The 32-kDa movement protein, P3, of alfalfa mosaic virus (AMV) is essential for cell-to-cell spread of the virus in plants. P3 shares many properties with other virus movement proteins (MPs); however, it is not known if P3 is posttranslationally modified by phosphorylation, which is important for the function of other MPs. When expressed in Nicotiana tabacum, P3 accumulated primarily in the cell walls of older leaves or in the cytosol of younger leaves. When expressed in Pischia pastoris, P3 accumulated primarily in a soluble form. Metabolic labeling indicated that a portion of P3 was phosphorylated in both tobacco and yeast, suggesting that phosphorylation regulates the function of this protein as it does for other virus MPs.
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