אסיף מאגר המחקר החקלאי

Domains of the TMV movement protein involved in subcellular localization

Year:

1998

Source of publication :

Authors :

Volume :

15

Co-Authors:

Kahn, T.W., Department of Cell Biology, Division of Plant Biology, Scripps Research Institute, 10550 North Torrey Pines Road, San Diego, CA 92037, United States, Pioneeer Hi-Bred International, Inc., 7300 N.W. 62nd Avenue, Johnston, IA 50131-1004, United States
Lapidot, M., Department of Cell Biology, Division of Plant Biology, Scripps Research Institute, 10550 North Torrey Pines Road, San Diego, CA 92037, United States, Department of Virology, Volcani Center, Box 6, Bet Dagan 50250, Israel
Heinlein, M., Department of Cell Biology, Division of Plant Biology, Scripps Research Institute, 10550 North Torrey Pines Road, San Diego, CA 92037, United States, Friedrich Miescher-Institut, Maulbeerstrasse 66, CH-4058 Basel, Switzerland
Reichel, C., Department of Cell Biology, Division of Plant Biology, Scripps Research Institute, 10550 North Torrey Pines Road, San Diego, CA 92037, United States
Cooper, B., Department of Cell Biology, Division of Plant Biology, Scripps Research Institute, 10550 North Torrey Pines Road, San Diego, CA 92037, United States, Department of Plant Pathology, University of California, Riverside, CA 92521, United States
Gafny, R., Department of Cell Biology, Division of Plant Biology, Scripps Research Institute, 10550 North Torrey Pines Road, San Diego, CA 92037, United States, Department of Virology, Volcani Center, Box 6, Bet Dagan 50250, Israel
Beachy, R.N., Department of Cell Biology, Division of Plant Biology, Scripps Research Institute, 10550 North Torrey Pines Road, San Diego, CA 92037, United States

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Abstract:

To identify and map functionally important regions of the tobacco mosaic virus movement protein, deletions of three amino acids were introduced at intervals of 10 amino acids throughout the protein. Mutations located between amino acids 1 and 160 abolished the capacity of the protein to transport virus from cell to cell, while some of the mutations in the C-terminal third of the protein permitted function. Despite extensive tests, no examples were found of intermolecular complementation between mutants, suggesting that function requires each movement protein molecule to be fully competent. Many of the mutants were fused to green fluorescent protein, and their subcellular localizations were determined by fluorescence microscopy in infected plants and protoplasts. Most mutants lost the ability to accumulate in one or more of the multiple subcellular sites targeted by wild-type movement protein, suggesting that specific functional domains were disrupted. The order in which accumulation at subcellular sites occurs during infection does not represent a targeting pathway. Association of the movement protein with microtubules or with plasmodesmata can occur in the absence of other associations. The region of the protein around amino acids 9-11 may be involved in targeting the protein to cortical bodies (probably associated with the endoplasmic reticulum) and to plasmodesmata. The region around residues 49-51 may be involved in co-alignment of the protein with microtubules. The region around residues 88-101 appears to play a role in targeting to both the cortical bodies and microtubules. Thus, the movement protein contains independently functional domains.

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