Differential Protein Metabolism and Gene Expression in Tomato Fruit during Wounding Stress
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概要
- 論文の詳細を見る
Changes in protein and RNA levels which occur in tomato (Lycopersicon esculentum cv. Pik-red) fruit tissue upon wounding were analyzed. Antibodies to nine plant proteins were used to identify the related cross-reactive proteins in tomato fruit tissue and quantify their abundance during wounding. Antibodies tested were pathogenesis-related proteins (PR-1a, 1b, 1c; PR-2, N, O; PR-P, Q; basic chitinase), plastid proteins (sorbitol-6-phosphate dehydrogenase; acyl carrier protein; large subunit of Rubisco), cellulase and 33-kD cationic peroxidase. Marked differences in mRNA populations were also detected when the protein translation products following in vitro translation of poly(A)^+ RNAs isolated from unwounded and wounded fruit tissue were compared. More direct evidence for the changes in mRNA levels was obtained by using specific cDNA probes, isolated from a cDNA library of wounded tomato pericarp tissue. Two cDNA clones identified RNAs that were induced upon wounding while a third cDNA clone identified a transcript whose abundance decreased.
- 日本植物生理学会の論文
著者
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Mattoo Autar
Department Of Biological Sciences University Of Maryland Baltimore County
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Mehta R
Ars Usda Md Usa
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Parsons B
Ars Usda Md Usa
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Mehta Roshni
Plant Molecular Biology Laboratory, Beltsville Agricultural Research Center
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Parsons Barbara
Department of Biological Sciences, University of Maryland Baltimore County
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Mehta Arkesh
Department of Biological Sciences, University of Maryland Baltimore County
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Nakhasi Hira
Institute of Biologics, FDA. Bethesda
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Mehta Arkesh
Department Of Biological Sciences University Of Maryland Baltimore County
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Nakhasi Hira
Institute Of Biologics Fda. Bethesda
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Mehta Roshni
Plant Molecular Biology Laboratory Beltsville Agricultural Research Center:department Of Bioiogical
関連論文
- Differential Protein Metabolism and Gene Expression in Tomato Fruit during Wounding Stress
- Tomato (Lycopersicon esculentum cv. Pik-Red) Leaf Carboxypeptidase: Identification, N-terminal Sequence, Stress-Regulation, and Specific Localization in the Paraveinal Mesophyll Vacuoles