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Journal of Virology, August 1999, p. 6831-6840, Vol. 73, No. 8
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Phosphorylation and/or Presence of Serine 37 in the Movement Protein of Tomato Mosaic Tobamovirus Is Essential for Intracellular Localization and Stability In Vivo

Shigeki Kawakami,1,3 Hal S. Padgett,2 Daijiro Hosokawa,3 Yoshimi Okada,4 Roger N. Beachy,5 and Yuichiro Watanabe1,*

Department of Life Sciences, Graduate School of Arts and Sciences, Meguro-ku, Tokyo 153-8902,1 Faculty of Agriculture, Tokyo University of Agriculture and Engineering, Fuchu, Tokyo 183-0054,3 and Department of Bioscience, School of Science and Engineering, Teikyo University, Utsunomiya 320-0003,4 Japan; Biosource Technologies, Inc., Vacaville, California 956882; and Danforth Plant Science Center, St. Louis, Missouri 631055

Received 1 December 1997/Accepted 20 April 1999

The P30 movement protein (MP) of tomato mosaic tobamovirus (ToMV) is synthesized in the early stages of infection and is phosphorylated in vivo. Here, we determined that serine 37 and serine 238 in the ToMV MP are sites of phosphorylation. MP mutants in which serine was replaced by alanine at positions 37 and 238 (LQ37A238A) or at position 37 only (LQ37A) were not phosphorylated, and mutant viruses did not infect tobacco or tomato plants. By contrast, mutation of serine 238 to alanine did not affect the infectivity of the virus (LQ238A). To investigate the subcellular localization of mutant MPs, we constructed viruses that expressed each mutant MP fused with the green fluorescent protein (GFP) of Aequorea victoria. Wild-type and mutant LQ238A MP fusion proteins showed distinct temporally regulated patterns of MP-GFP localization in protoplasts and formation of fluorescent ring-shaped infection sites on Nicotiana benthamiana. However mutant virus LQ37A MP-GFP did not show a distinct pattern of localization or formation of fluorescent rings. Pulse-chase experiments revealed that MP produced by mutant virus LQ37A was less stable than wild-type and LQ238A MPs. MP which contained threonine at position 37 was phosphorylated, but the stability of the MP in vivo was very low. These studies suggest that the presence of serine at position 37 or phosphorylation of serine 37 is essential for intracellular localization and stability of the MP, which is necessary for the protein to function.

* Corresponding author. Mailing address: Department of Life Sciences, Graduate School of Arts and Sciences, Komaba 3-8-1, Meguro-ku, Tokyo 153-8902, Japan. Phone: 81-3-5454-6776. Fax: 81-3-5454-6776. E-mail: cyuiwat{at}komaba.ecc.u-tokyo.ac.jp.

Journal of Virology, August 1999, p. 6831-6840, Vol. 73, No. 8
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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