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Actin Depolymerization Affects Stress-Induced Translational Activity of Potato Tuber Tissue1

James K. Morelli2, Wei Zhou3, Jia Yu, Chen Lu, and Michael E. Vayda*

Department of Biochemistry, Microbiology and Molecular Biology, University of Maine, Orono, Maine 04469-5735

Changes in polymerized actin during stress conditions were correlated with potato (Solanum tuberosum L.) tuber protein synthesis. Fluorescence microscopy and immunoblot analyses indicated that filamentous actin was nearly undetectable in mature, quiescent aerobic tubers. Mechanical wounding of postharvest tubers resulted in a localized increase of polymerized actin, and microfilament bundles were visible in cells of the wounded periderm within 12 h after wounding. During this same period translational activity increased 8-fold. By contrast, low-oxygen stress caused rapid reduction of polymerized actin coincident with acute inhibition of protein synthesis. Treatment of aerobic tubers with cytochalasin D, an agent that disrupts actin filaments, reduced wound-induced protein synthesis in vivo. This effect was not observed when colchicine, an agent that depolymerizes microtubules, was used. Neither of these drugs had a significant effect in vitro on run-off translation of isolated polysomes. However, cytochalasin D did reduce translational competence in vitro of a crude cellular fraction containing both polysomes and cytoskeletal elements. These results demonstrate the dependence of wound-induced protein synthesis on the integrity of microfilaments and suggest that the dynamics of the actin cytoskeleton may affect translational activity during stress conditions.

1   This work was supported by the U.S. Department of Agriculture-National Research Initiative Grant Program (grant no. 95-37100-1564) and the Maine Agricultural and Forestry Experiment Station Project (grant no. ME38402). This is publication no. 2180 of the Maine Agricultural and Forestry Experiment Station.
2   Present address: Zeneca, Inc., 1800 Concord Pike, Wilmington, DE 19850.
3   Present address: Department of Plant Pathology and Microbiology, Texas A&M University, College Station, TX 77840.
*   Corresponding author; e-mail vayda{at}maine.maine.edu; fax 1-207-581-2801.

Plant Physiol. (1998) 116: 1227-1237
Copyright Clearance Center:   0032-0889/98/116/1227/11
© 1998 American Society of Plant Physiologists




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