文献类型： 外文期刊
作者： Wei, Jia 1 ; Qiu, Xiaoyun 1 ; Chen, Lin 1 ; Hu, Wenjun 1 ; Hu, Rongbin 2 ; Chen, Jian 2 ; Sun, Li 2 ; Li, Li 3 ; Zhang, Hong 2 ;
作者机构： 1.Zhejiang Acad Agr Sci, Hangzhou 310021, Zhejiang, Peoples R China
2.Texas Tech Univ, Dept Biol Sci, Lubbock, TX 79409 USA
3.Cornell Univ, Robert W Holley Ctr Agr & Hlth, USDA ARS, Ithaca, NY 14853 USA
4.Cornell Univ, Dept Plant Breeding & Genet, Ithaca, NY 14853 USA
关键词： AtCHIP;chloroplast protease;Clp proteolytic subunits;ClpP4;ClpP3;ClpP5;protein homeostasis
期刊名称：JOURNAL OF EXPERIMENTAL BOTANY （ 影响因子：6.992； 五年影响因子：7.86 ）
ISSN：
年卷期：
页码：
收录情况： SCI
摘要： AtCHIP positively regulates Clp subunit degradation by selective ubiquitylation of their precursors in cytosol, providing new evidence for the E3 ligase-based proteasome system regulating nuclear-encoded organelle protein biogenesis and homeostasis.The caseinolytic peptidase (Clp) core proteins are essential for plant growth and development, especially for chloroplast function. Antisense or overexpression of ClpP4, which is one of the Clp core subunits, causes chlorotic phenotypes in Arabidopsis. An E3 ligase gene, AtCHIP, has previously been found to ubiquitylate ClpP4 in vitro. ClpP4 antisense and overexpressing plants that also overexpressed AtCHIP were constructed to explore the effect of AtCHIP on ClpP4. Overexpression of AtCHIP was found to rescue the chlorotic phenotypes of both ClpP4 antisense and overexpressing plants. The unbalanced levels of Clp core proteins in ClpP4 antisense and overexpressing plants with overexpression of AtCHIP were similar to wild-type levels, suggesting that AtCHIP regulates Clp core proteins. The results also show that AtCHIP can interact with ClpP3 and ClpP5 in yeast and ubiquitylate ClpP3 and ClpP5 in vitro. This suggests that AtCHIP is directly related to ClpP3 and ClpP5. Given these results, the inference is that through selective degradation of Clp subunits, AtCHIP could positively regulate homeostasis of Clp proteolytic subunits and maximize the production of functional chloroplasts. Similar results were obtained from transgenic tobacco plants, suggesting that regulation of the Clp protease by AtCHIP is conserved.
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