Phosphorylation of alfalfa mosaic virus movement protein in vivo

Phosphorylation of alfalfa mosaic virus movement protein in vivo 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Virology Springer Journals

Phosphorylation of alfalfa mosaic virus movement protein in vivo

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Publisher
Springer Journals
Copyright
Copyright © 2014 by Springer-Verlag Wien
Subject
Biomedicine; Virology; Medical Microbiology; Infectious Diseases
ISSN
0304-8608
eISSN
1432-8798
D.O.I.
10.1007/s00705-013-1945-7
Publisher site
See Article on Publisher Site

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.

Journal

Archives of VirologySpringer Journals

Published: Jul 1, 2014

References

  • Phosphorylation and interaction of the movement and coat proteins of brome mosaic virus in infected barley protoplasts
    Akamatsu, N; Takeda, A; Kishimoto, M; Kaido, M; Okuno, T; Mise, K
  • Arabidopsis thaliana is an asymptomatic host of Alfalfa mosaic virus
    Balasubramaniam, M; Ibrahim, A; Kim, BS; Loesch-Fries, LS
  • Plant protein serine/threonine kinases: classification and functions
    Hardie, DG
  • Phosphorylation events during viral infections provide potential therapeutic targets
    Keating, JA; Striker, R
  • Post-translational modifications of Abutilon mosaic virus movement protein (BC1) in fission yeast
    Kleinow, T; Holeiter, G; Nischang, M; Stein, M; Karayavuz, M; Wege, C; Jeske, H
  • Plasmodesmata: intercellular tunnels facilitating transport of macromolecules in plants
    Kragler, F
  • Phosphorylation of the movement protein of Cucumber mosaic virus in transgenic tobacco plants
    Matsushita, Y; Yoshioka, K; Shigyo, T; Takahashi, H; Nyunoy, H
  • Phosphorylation of the TGBp1 movement protein of Potato virus X by a Nicotiana tabacum CK2-like activity
    Modena, NA; Zelada, AM; Conte, F; Mentaberry, A
  • Reciprocal phosphorylation and glycosylation recognition motifs control NCAPP1 interaction with pumpkin phloem proteins and their cell-to-cell movement
    Taoka, K; Ham, BK; Xoconostle-Cazares, B; Rojas, MR; Lucas, WJ

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