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פותח על ידי קלירמאש פתרונות בע"מ -
The TMV movement protein: Role of the C-terminal 73 amino acids in subcellular localization and function
Year:
1991
Source of publication :
Virology
Authors :
גפני, רון
;
.
Volume :
182
Co-Authors:
Berna, A., Université Laval, Département de Biochimie, Ste-Foy, Québec, Canada, G 1 K 7P4
Gafny, R., Washington University, Department of Biology, PO Box 1137, St. Louis, MO 63130, United States
Wolf, S., University of California, Botany Department, Davis, CA 95616, United States
Lucas, W.J., University of California, Botany Department, Davis, CA 95616, United States
Holt, C.A., Washington University, Department of Biology, PO Box 1137, St. Louis, MO 63130, United States
Beachy, R.N., Washington University, Department of Biology, PO Box 1137, St. Louis, MO 63130, United States
Facilitators :
From page:
682
To page:
689
(
Total pages:
8
)
Abstract:
The role of the C-terminal one-third of the tobacco mosaic virus (TMV) 30-kDa movement protein (MP) on its subcellular localization and on virus spread was investigated. We have constructed eight cDNAs encoding MPs with variable size deletions from the C-terminal end. Expression of the truncated proteins was verified in recombinant yeast using an antiserum directed to a synthetic peptide corresponding to 21 amino acids near the N-terminal end of the MP. In transgenic tobacco plants, MP from which more than 55 amino acids were deleted no longer accumulated in the cell wall fraction of a cellular extract, where the complete MP accumulates. Dye diffusion studies showed that both unmodified and modified MPs that accumulate in the cell wall fraction are able to alter plasmodesmatal size exclusion limits. Biological function of the modified MPs was tested in the transgenic plants with the TMV thermosensitive mutant Lsl and a TMV genomic RNA transcript lacking a functional MP. There was a correlation between the cell wall localization of the modified MPs and its ability to potentiate virus spread. The results presented here demonstrate the dispensability of the C-terminal 55 amino acids of the MP in its subcellular localization in tobacco plants and its role in virus movement. Moreover, our results show that a stretch of 19 amino acids (195 to 213) is essential for localization of the MP to the cell wall fraction of plant cells. © 1991.
Note:
Related Files :
DNA
gene expression
Nicotiana obtusifolia
Plant Diseases
Plants, Toxic
Tobacco mosaic virus
Yeast
עוד תגיות
תוכן קשור
More details
DOI :
10.1016/0042-6822(91)90609-F
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
26898
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:26
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Scientific Publication
The TMV movement protein: Role of the C-terminal 73 amino acids in subcellular localization and function
182
Berna, A., Université Laval, Département de Biochimie, Ste-Foy, Québec, Canada, G 1 K 7P4
Gafny, R., Washington University, Department of Biology, PO Box 1137, St. Louis, MO 63130, United States
Wolf, S., University of California, Botany Department, Davis, CA 95616, United States
Lucas, W.J., University of California, Botany Department, Davis, CA 95616, United States
Holt, C.A., Washington University, Department of Biology, PO Box 1137, St. Louis, MO 63130, United States
Beachy, R.N., Washington University, Department of Biology, PO Box 1137, St. Louis, MO 63130, United States
The TMV movement protein: Role of the C-terminal 73 amino acids in subcellular localization and function
The role of the C-terminal one-third of the tobacco mosaic virus (TMV) 30-kDa movement protein (MP) on its subcellular localization and on virus spread was investigated. We have constructed eight cDNAs encoding MPs with variable size deletions from the C-terminal end. Expression of the truncated proteins was verified in recombinant yeast using an antiserum directed to a synthetic peptide corresponding to 21 amino acids near the N-terminal end of the MP. In transgenic tobacco plants, MP from which more than 55 amino acids were deleted no longer accumulated in the cell wall fraction of a cellular extract, where the complete MP accumulates. Dye diffusion studies showed that both unmodified and modified MPs that accumulate in the cell wall fraction are able to alter plasmodesmatal size exclusion limits. Biological function of the modified MPs was tested in the transgenic plants with the TMV thermosensitive mutant Lsl and a TMV genomic RNA transcript lacking a functional MP. There was a correlation between the cell wall localization of the modified MPs and its ability to potentiate virus spread. The results presented here demonstrate the dispensability of the C-terminal 55 amino acids of the MP in its subcellular localization in tobacco plants and its role in virus movement. Moreover, our results show that a stretch of 19 amino acids (195 to 213) is essential for localization of the MP to the cell wall fraction of plant cells. © 1991.
Scientific Publication
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