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Mol. Cells 2012; 33(1): 99-103

Published online January 2, 2012

https://doi.org/10.1007/s10059-012-2245-x

© The Korean Society for Molecular and Cellular Biology

Giant Chloroplast Development in ethylene response1-1 Is Caused by a Second Mutation in ACCUMULATION AND REPLICATION OF CHLOROPLAST3 in Arabidopsis

Young-Hee Cho1, Geun-Don Kim1, and Sang-Dong Yoo*

Department of Biological Science, SungKyunKwan University, Suwon 440-746, Korea, 1These authors contributed equally to this work.

Correspondence to : *Correspondence: sangdong@skku.edu

Received: October 31, 2011; Accepted: November 7, 2011

Abstract

The higher plants of today array a large number of small chloroplasts in their photosynthetic cells. This array of small chloroplasts results from organelle division via prokaryotic binary fission in a eukaryotic plant cell environment. Functional abnormalities of the tightly coordinated biochemical event of chloroplast division lead to abnormal chloroplast development in plants. Here, we described an abnormal chloroplast phenotype in an ethylene insensitive ethylene response1-1 (etr1-1) of Arabidopsis thaliana. Extensive transgenic and genetic analyses revealed that this organelle abnormality was not linked to etr1-1 or ethylene signaling, but linked to a sec-ond mutation in ACCUMULA-TION AND REPLICATION3 (ARC3), which was further verified by genetic complementation analysis. Despite the normal expression of other plastid division-related genes, the loss of ARC3 caused the enlargement of chloroplasts as well as the diminution of a photosynthetic protein Rubisco in etr1-1. Our study has suggested that the in-creased size of the abnormal chloroplasts may not be able to fully compensate for the loss of a greater array of small chloroplasts in higher plants.

Keywords arc3-3, etr1-1, giant chloroplast

Article

Research Article

Mol. Cells 2012; 33(1): 99-103

Published online January 31, 2012 https://doi.org/10.1007/s10059-012-2245-x

Copyright © The Korean Society for Molecular and Cellular Biology.

Giant Chloroplast Development in ethylene response1-1 Is Caused by a Second Mutation in ACCUMULATION AND REPLICATION OF CHLOROPLAST3 in Arabidopsis

Young-Hee Cho1, Geun-Don Kim1, and Sang-Dong Yoo*

Department of Biological Science, SungKyunKwan University, Suwon 440-746, Korea, 1These authors contributed equally to this work.

Correspondence to:*Correspondence: sangdong@skku.edu

Received: October 31, 2011; Accepted: November 7, 2011

Abstract

The higher plants of today array a large number of small chloroplasts in their photosynthetic cells. This array of small chloroplasts results from organelle division via prokaryotic binary fission in a eukaryotic plant cell environment. Functional abnormalities of the tightly coordinated biochemical event of chloroplast division lead to abnormal chloroplast development in plants. Here, we described an abnormal chloroplast phenotype in an ethylene insensitive ethylene response1-1 (etr1-1) of Arabidopsis thaliana. Extensive transgenic and genetic analyses revealed that this organelle abnormality was not linked to etr1-1 or ethylene signaling, but linked to a sec-ond mutation in ACCUMULA-TION AND REPLICATION3 (ARC3), which was further verified by genetic complementation analysis. Despite the normal expression of other plastid division-related genes, the loss of ARC3 caused the enlargement of chloroplasts as well as the diminution of a photosynthetic protein Rubisco in etr1-1. Our study has suggested that the in-creased size of the abnormal chloroplasts may not be able to fully compensate for the loss of a greater array of small chloroplasts in higher plants.

Keywords: arc3-3, etr1-1, giant chloroplast

Mol. Cells
Jun 30, 2023 Vol.46 No.6, pp. 329~398
COVER PICTURE
The cellular proteostasis network is adaptively modulated upon cellular stress, thereby protecting cells from proteostasis collapse. Heat shock induces the translocation of misfolded proteins and the chaperone protein HSP70 into nucleolus, where nuclear protein quality control primarily occurs. Nuclear RNA export factor 1 (green), nucleolar protein fibrillarin (red), and nuclei (blue) were visualized in NIH3T3 cells under basal (left) and heat shock (right) conditions (Park et al., pp. 374-386).

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