Enhanced chloroplast FtsZ-ring constriction by the ARC6-ARC3 module in Arabidopsis

• 成果类型: Article
• 署名作者: Du, Wenbin; Cao, Lingyan; Zhou, Yuelong; Jackson, Shanelle; Naeem, Maryam; Chen, Zhaoyu; Yang, Yue; Glynn, Jonathan M.; Porter, Katie J.; Zhang, Runlong; He, Qian; Liu, Moyang; Xu, Jie; Liang, Wanqi; Feng, Peiqiang; Osteryoung, Katherine W.; Chen, Cheng
• 署名单位: Jiangxi Agricultural University; Pfizer; Pfizer USA; Shanghai Jiao Tong University; Shanghai Jiao Tong University; Michigan State University; Chinese Academy of Sciences; Center for Excellence in Molecular Plant Sciences, CAS; Shanghai Jiao Tong University; Shanghai Jiao Tong University; Shanghai Jiao Tong University
• 刊物名称: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
• ISSN/ISSBN: 0027-9874
• DOI: 10.1073/pnas.2425129122
• 发表日期: 2025-07-01
• 关键词: plastid division proteins; cell-division; escherichia-coli; assembly dynamics; bacterial; arc3; machinery; complex; site; COORDINATION

摘要

Chloroplast division, a process tightly linked to the energy demands of plants, is initiated by the formation of the stromal filamenting temperature-sensitive Z (FtsZ) ring. The Z ring is highly dynamic, and its constriction provides the essential force for chloroplast division. However, the regulatory mechanisms governing Z-ring dynamics and constriction remain poorly understood. Here, we report that the chloroplast inner envelope membrane (IEM) protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS6 (ARC6) interacts with the chloroplast stromal protein ARC3, and this interaction is negatively regulated by the conserved J-like domain ofARC6. ARC3 is found both distributed throughout the stroma and localized to a ring-like structure at the chloroplast division site. We demonstrate that ARC6 recruits ARC3 to the division site to form a ring-like structure, likely through direct interaction. This ARC6-ARC3 interaction enables ARC3 to bind FtsZs. Furthermore, we show that the ARC6-ARC3 complex significantly promotes the dynamics of chloroplast Z rings reconstituted in a heterologous system. Finally, the constriction of these reconstituted Z rings is markedly enhanced by ARC6-ARC3. Our findings reveal a regulatory mechanism that governs Z-ring dynamics and constriction, shedding light on the molecular mechanisms underlying chloroplast division.