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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/37732

Title: Plastidial Starch Phosphorylase in Sweet Potato Roots Is Proteolytically Modified by Protein-Protein Interaction with the 20S Proteasome
Authors: Yi-Chen Lin;Han-Min Chen;I-Min Chou;An-Na Chen;Chia-Pei Chen;Guang-Huar Young;Chi-Tsai Lin;Chiung-Hsiang Cheng;Shih-Chung Chang;Rong-Huay Juang
Contributors: 國立台灣海洋大學:生命科學系
Date: 2012
Issue Date: 2016-05-02T06:45:54Z
Publisher: RESEARCH ARTICLE
Abstract: Abstract:Post-translational regulation plays an important role in cellular metabolism. Earlier studies showed that the activity of plastidial starch phosphorylase (Pho1) may be regulated by proteolytic modification. During the purification of Pho1 from sweet potato roots, we observed an unknown high molecular weight complex (HX) showing Pho1 activity. The two-dimensional gel electrophoresis, mass spectrometry, and reverse immunoprecipitation analyses showed that HX is composed of Pho1 and the 20S proteasome. Incubating sweet potato roots at 45°C triggers a stepwise degradation of Pho1; however, the degradation process can be partially inhibited by specific proteasome inhibitor MG132. The proteolytically modified Pho1 displays a lower binding affinity toward glucose 1-phosphate and a reduced starch-synthesizing activity. This study suggests that the 20S proteasome interacts with Pho1 and is involved in the regulation of the catalytic activity of Pho1 in sweet potato roots under heat stress conditions.
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/37732
Appears in Collections:[生命科學系] 期刊論文

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