An Arabidopsis Pentatricopeptide Repeat Protein, SUPPRESSOR OF VARIEGATION7, Is Required for FtsH-Mediated Chloroplast Biogenesis

Author:

Liu Xiayan1,Yu Fei1,Rodermel Steve1

Affiliation:

1. Department of Genetics, Development, and Cell Biology (X.L., S.R.) and Interdepartmental Genetics Graduate Program (X.L.), Iowa State University, Ames, Iowa 50011; and College of Life Sciences, Northwest A&F University, Yangling, Shaanxi 712100, People's Republic of China (F.Y.)

Abstract

Abstract The Arabidopsis (Arabidopsis thaliana) yellow variegated2 (var2) mutant has green- and white-sectored leaves due to loss of VAR2, a subunit of the chloroplast FtsH protease/chaperone complex. Suppressor screens are a valuable tool to gain insight into VAR2 function and the mechanism of var2 variegation. Here, we report the molecular characterization of 004-003, a line in which var2 variegation is suppressed. We found that the suppression phenotype in this line is caused by lack of a chloroplast pentatricopeptide repeat (PPR) protein that we named SUPPRESSOR OF VARIEGATION7 (SVR7). PPR proteins contain tandemly repeated PPR motifs that bind specific RNAs, and they are thought to be central regulators of chloroplast and mitochondrial nucleic acid metabolism in plants. The svr7 mutant has defects in chloroplast ribosomal RNA (rRNA) processing that are different from those in other svr mutants, and these defects are correlated with reductions in the accumulation of some chloroplast proteins, directly or indirectly. We also found that whereas var2 displays a leaf variegation phenotype at 22°C, it has a pronounced chlorosis phenotype at 8°C that is correlated with defects in chloroplast rRNA processing and a drastic reduction in chloroplast protein accumulation. Surprisingly, the cold-induced phenotype of var2 cannot be suppressed by svr7. Our results strengthen the previously established linkage between var2 variegation and chloroplast rRNA processing/chloroplast translation, and they also point toward the possibility that VAR2 mediates different activities in chloroplast biogenesis at normal and chilling temperatures.

Publisher

Oxford University Press (OUP)

Subject

Plant Science,Genetics,Physiology

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