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Changes in the Number and Composition of Chloroplasts During Senescence of Mesophyll Cells of Attached and Detached Primary Leaves of Wheat (Triticum Aestivum L.)

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Journal Plant Physiol
Specialty Physiology
Date 1984 Jun 1
PMID 16663637
Citations 12
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Abstract

Changes in the number and composition of chloroplasts of mesophyll cells were followed during senescence of the primary leaf of wheat (Triticum aestivum L.). Senescence was due to the natural pattern of leaf ontogeny or was either induced by leaf detachment and incubation in darkness, or incubation of attached leaves in the dark. In each case discrete sections (1 centimeter) of the leaf, representing mesophyll cells of the basal, middle, and tip regions, were examined. For all treatments, senescence was characterized by a loss of chlorophyll and the protein ribulose 1,5-bisphosphate carboxylase (RuBPCase). Chloroplast number per mesophyll cell remained essentially constant during senescence. It was not until more than 80% of the plastid chlorophyll and RuBPCase was degraded that some reduction (22%) in chloroplast number per mesophyll cell was recorded and this was invariably in the mesophyll cells of the leaf tip. We conclude that these data are consistent with the idea that degradation occurs within the chloroplast and that all chloroplasts in a mesophyll cell senesce with a high degree of synchrony rather than each chloroplast senescing sequentially.

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References
1.
Bradford M . A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976; 72:248-54. DOI: 10.1016/0003-2697(76)90527-3. View

2.
Boller T, Kende H . Hydrolytic enzymes in the central vacuole of plant cells. Plant Physiol. 1979; 63(6):1123-32. PMC: 542982. DOI: 10.1104/pp.63.6.1123. View

3.
Waters S, NOBLE E, Dalling M . Intracellular Localization of Peptide Hydrolases in Wheat (Triticum aestivum L.) Leaves. Plant Physiol. 1982; 69(3):575-9. PMC: 426257. DOI: 10.1104/pp.69.3.575. View

4.
Wittenbach V, Lin W, Hebert R . Vacuolar localization of proteases and degradation of chloroplasts in mesophyll protoplasts from senescing primary wheat leaves. Plant Physiol. 1982; 69(1):98-102. PMC: 426153. DOI: 10.1104/pp.69.1.98. View

5.
Lin W, Wittenbach V . Subcellular localization of proteases in wheat and corn mesophyll protoplasts. Plant Physiol. 1981; 67(5):969-72. PMC: 425811. DOI: 10.1104/pp.67.5.969. View