한빛사논문
- 조회459
Sam-Geun Kong 1 2, Yosuke Yamazaki 3 4, Atsushi Shimada 5, Saku T Kijima 6, Keiko Hirose 6, Kaoru Katoh 6, Jeongsu Ahn 1, Hyun-Geun Song 1, Jae-Woo Han 1, Takeshi Higa 7, Akira Takano 5, Yuki Nakamura 5, Noriyuki Suetsugu 2, Daisuke Kohda 5, Taro Q P Uyeda 3 6, Masamitsu Wada 2 8 *
1Department of Biological Sciences, College of Natural Sciences, Kongju National University, Chungnam 32588, Korea.
2Department of Biology, Faculty of Sciences, Kyushu University, Fukuoka 812-8581, Japan.
3Department of Physics, Faculty of Science and Engineering, Waseda University, Tokyo 169-8555, Japan.
4Department of Physics, Graduate School of Science, Kyoto University, Kyoto, 606-8502, Japan.
5Division of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, Japan.
6Biomedical Research Institute, National Institute of Advanced Industrial Science and Technology, Ibaraki 305-8562, Japan.
7Institute for Protein Research, Osaka University, Osaka 565-0871, Japan.
8Graduate School of Science, Tokyo Metropolitan University, Tokyo 192-0397, Japan.
*Corresponding author: correspondence to Masamitsu Wada
Abstract
Plants have unique responses to fluctuating light conditions. One such response involves chloroplast photorelocation movement, which optimizes photosynthesis under weak light by the accumulation of chloroplasts along the periclinal side of the cell, which prevents photodamage under strong light by avoiding chloroplast positioning toward the anticlinal side of the cell. This light-responsive chloroplast movement relies on the reorganization of chloroplast actin (cp-actin) filaments. Previous studies have suggested that CHLOROPLAST UNUSUAL POSITIONING 1 (CHUP1) is essential for chloroplast photorelocation movement as a regulator of cp-actin filaments. In this study, we conducted comprehensive analyses to understand CHUP1 function. Functional, fluorescently-tagged CHUP1 colocalized with and was coordinately reorganized with cp-actin filaments on the chloroplast outer envelope during chloroplast movement in Arabidopsis thaliana. CHUP1 distribution was reversibly regulated in a blue light- and phototropin-dependent manner. X-ray crystallography revealed that the CHUP1 C-terminal domain shares structural homology with the formin homology 2 (FH2) domain, despite lacking sequence similarity. Furthermore, the CHUP1 C-terminal domain promoted actin polymerization in the presence of profilin in vitro. Taken together, our findings indicate that CHUP1 is a plant-specific actin polymerization factor that has convergently evolved to assemble cp-actin filaments and enables chloroplast photorelocation movement.
논문정보
- Research article
- 2023년 12월 (BRIC 등록일 2024-01-02)
- 국내+국외 연구진
- 생명과학 > 식물학
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