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OsNOA1/RIF1 is a functional homolog of AtNOA1/RIF1: implication for a highly conserved plant cGTPase essential for chloroplast function

文献类型： 外文期刊

作者： Liu, Hongjia 1 ; Lau, Edward 3 ; Lam, Maggie P. Y. 3 ; Chu, Hung 2 ; Li, Sujuan 1 ; Huang, Guo 1 ; Guo, Peng 1 ; Wang, Ju 1 ;

作者机构： 1.Zhejiang Acad Agr Sci, Crop Mol Breeding Ctr, Hangzhou, Zhejiang, Peoples R China

2.Univ Hong Kong, Sch Biol Sci, Hong Kong, Hong Kong, Peoples R China

3.Univ Hong Kong, Dept Chem, Hong Kong, Hong Kong, Peoples R China

4.Chinese Univ Hong Kong, Dept Biol, Shatin, Hong Kong, Peoples R China

关键词： Molecular Genetics: Biochemistry and Molecular Biophysics;Enzymology: Biochemistry and Molecular Biophysics;Cell Biology;Agronomy: Agriculture

期刊名称：NEW PHYTOLOGIST （ 影响因子：10.151； 五年影响因子：10.475 ）

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收录情况： SCI

摘要： P>The bacterial protein YqeH is a circularly permuted GTPase with homologs encoded by plant nuclear genomes. The rice homolog OsNOA1/RIF1 is encoded by the single-copy gene Os02g01440. OsNOA1/RIF1 is expressed in different tissues and is light-inducible. The OsNOA1/RIF1-EYFP fusion protein was targeted to chloroplasts in transgenic Arabidopsis plants. In addition, the rice homolog was able to rescue most of the growth phenotypes in an Arabidopsis rif1 mutant.Rice (Oryza sativa) OsNOA1/RIF1 RNAi mutant seedlings were chlorotic with reduced pigment contents and lower photosystem II (PSII) efficiency. However, the expressions of the chloroplast-encoded genes rbcL, atpB, psaA and psbA were not affected. By contrast, reduced abundance of the chloroplast 16S rRNA was observed in the mutant.Quantitative iTRAQ-LC-MS/MS proteomics investigations revealed proteome changes in the rice mutant consistent with the expected functional role of OsNOA1/RIF1 in chloroplast translation. The RNAi mutant showed significantly decreased expression levels of chloroplast-encoded proteins as well as nuclear-encoded components of chloroplast enzyme complexes. Conversely, upregulation of some classes of nonchloroplastic proteins, such as glycolytic and phenylpropanoid pathway enzymes, was detected.Our work provides independent indications that a highly conserved nuclear-encoded cGTPase of likely prokaryotic origin is essential for proper chloroplast ribosome assembly and/or translation in plants.

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