| ARTICLE ABSTRACT | |||||||
| DOI: 10.1099/vir.0.18972-0 | ||||||||
| Online 20 December 2002 | ||||||||
E. M. Karger,1 O. Yu. Frolova,1 N. V. Fedorova,1 L. A. Baratova,1 T. V. Ovchinnikova,2 P. Susi,3 K. Makinen,4 L. Ronnstrand,5 Yu. L. Dorokhov1 and J. G. Atabekov1
1Department of Virology and A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Vorobiovy Gory Moscow 119899, Russia
2M. M. Shemyakin and Yu. A. Ovchinnikov Institut of Bioorganic Chemistry, Moscow, Russia
3Joint Biotechnology Laboratory, Biocity, Turku, Finland
4University of Helsinki, Institute of Biotechnology, Biocenter, Helsinki, Finland
5Ludwig Institute of Cancer Research, Biomedical Center, Uppsala, Sweden
Replication of tobacco mosaic virus (TMV) is connected with endoplasmic reticulum (ER)-associated membranes at early stages of infection. This study reports that TMV movement protein (MP)-specific protein kinases (PKs) associated with the ER of tobacco were capable of phosphorylating Thr104 in TMV MP. The MP-specific PKs with apparent molecular masses of about 45–50 kDa and 38 kDa were revealed by gel PK assays. Two types of mutations were introduced in TMV MP gene of wild-type TMV U1 genome to substitute Thr104 by neutral Ala or by negatively charged Asp. Mutation of Thr104 to Ala did not affect the size of necrotic lesions induced by the mutant virus in Nicotiana tabacum Xanthi nc. plants. Conversely, mutation of Thr to Asp mimicking Thr104 phosphorylation strongly inhibited cell-to-cell movement. The possible role of Thr104 phosphorylation in TMV MP function is discussed.
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This article is now available in the March 2003 print issue of JGV (vol. 84, 727–732). The complete issue of the journal may be seen in electronic form on JGV Online.
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