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PLANT PHYSIOLOGY , Vol 111, Issue 4 1233-1241, Copyright © 1996 by American Society of Plant Biologists
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CELL BIOLOGY AND SIGNAL TRANSDUCTION |
Autophagy in Tobacco Suspension-Cultured Cells in Response to Sucrose Starvation
Y. Moriyasu and Y. Ohsumi
Department of Biology, Faculty of International Relations, University of Shizuoka, 52-1 Yada, Shizuoka-shi, Shizuoka 422, Japan (Y.M.)
The response of tobacco (Nicotiana tabacum) suspension-cultured cells
(BY-2) to nutrient starvation was investigated. When the cells that were
grown in Murashige-Skoog medium containing 3% (w/v) sucrose were
transferred to the same medium without sucrose, 30 to 45% of the
intracellular proteins were degraded in 2 d. An analysis with sodium
dodecyl sulfate-polyacrylamide gel electrophoresis showed that proteins
were degraded nonselectively. With the same treatment, protease activity in
the cell, which was measured at pH 5.0 using fluorescein
thiocarbamoyl-casein as a substrate, increased 3- to 7-fold after 1 d. When
the cysteine protease inhibitor
(2S,3S)-trans-epoxysuccinyl-L-leucylamido-3-methyl-butane (10 [mu]M) was
present in the starvation medium, both the protein degradation and the
increase in the protease activity were effectively inhibited. Light
microscopy analysis showed that many small spherical bodies accumulated in
the perinuclear region of the cytosol 8 h after the start of the inhibitor
treatment. These bodies were shown to be membrane-bound vesicles of 1 to 6
[mu]m in diameter that contained several particles. Quinacrine stained
these vesicles and the central vacuole; thus, both organelles are acidic
compartments. Cytochemical enzyme analysis using 1-naphthylphosphate and
[beta]-glycerophosphate as substrates showed that these vesicles contained
an acid phosphatase(s). We suggest that these vesicles contribute to
cellular protein degradation stimulated under sucrose starvation
conditions.
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