Interaction between ACC Synthase 1 and 14-3-3 Proteins in Rice: a New Insight

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Yuan Yao, Ying Du, Lin Jiang, and Jin-Yuan Liu^*

Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, P. R. China; fax: (86) 1062-772-243; E-mail: liujy@mail.tsinghua.edu.cn

^* To whom correspondence should be addressed.

Received March 6, 2007; Revision received May 9, 2007

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In this study, the interaction between rice 14-3-3 protein and 1-aminocyclopropane carboxylic acid synthase (ACS) was observed in yeast cells using yeast two-hybrid assays. Given the fact that 14-3-3 proteins generally bind to their target proteins in a phosphorylation-dependent manner, a hypothesis regarding the regulatory role of 14-3-3 proteins in the activation of ACS is proposed in which 14-3-3 proteins may bind to the phosphorylated C-terminal tails of ACSs and help them to escape from their fated degradation when ethylene biosynthesis is needed. It is reasonable to believe that 14-3-3 protein may play an important role in regulating ACS activity.

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KEY WORDS: Oryza sativa, ethylene biosynthesis, ACC synthase, 14-3-3 protein, yeast two-hybrid assay, hypothesis

DOI: 10.1134/S000629790709012X

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