Phosphorylation of alfalfa mosaic virus movement protein in vivo
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- 作者：Bong-Suk Kim (1)
Edward L. Halk (2) (3)
Donald J. Merlo (2) (4)
Steven E. Nelson (2) (5)
L. Sue Loesch-Fries (1) (2) - 刊名：Archives of Virology
- 出版年：2014
- 出版时间：July 2014
- 年：2014
- 卷：159
- 期：7
- 页码：1787-1791
- 全文大小：312 KB
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Edward L. Halk (2) (3)
Donald J. Merlo (2) (4)
Steven E. Nelson (2) (5)
L. Sue Loesch-Fries (1) (2)
1. Department of Botany and Plant Pathology, Purdue University, West Lafayette, IN, 47907, USA
2. Agrigenetics Advanced Science Company, Madison, WI, USA
3. Bristol-Myers Squibb, Redwood City, CA, USA
4. 11845 Durbin Drive, Carmel, IN, 46032, USA
5. 4397 Gils Way, Cross Plains, WI, 53528, USA - ISSN：1432-8798
文摘
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.