质体
生物
拟南芥
细菌外膜
细胞生物学
叶绿体膜
拟南芥
叶绿体
内膜
易位
突变体
膜蛋白
膜
生物化学
类囊体
基因
线粒体
大肠杆菌
作者
Ryo Yoshimura,Syun Minamikawa,Takamasa Suzuki,Kazuyoshi Goto,David Latrasse,Sanchari Sicar,Cécile Raynaud,Moussa Benhamed,Yasushi Yoshioka
出处
期刊:Plant Physiology
[Oxford University Press]
日期:2024-01-17
卷期号:194 (4): 2422-2433
标识
DOI:10.1093/plphys/kiae005
摘要
Abstract Embedded β-barrel proteins in the outer envelope membrane mediate most cellular trafficking between the cytoplasm and plastids. Although the TRANSLOCON AT THE OUTER ENVELOPE MEMBRANE OF CHLOROPLASTS 75-V (TOC75-V)/OUTER ENVELOPE PROTEIN OF 80 KDA (OEP80) complex has been implicated in the insertion and assembly of β-barrel proteins in the outer envelope membrane of Arabidopsis (Arabidopsis thaliana) chloroplasts, relatively little is known about this process. CRUMPLED LEAF (CRL) encodes a chloroplast outer envelope membrane-localized protein, and its loss-of-function mutation results in pleiotropic defects, including altered plant morphogenesis, growth retardation, suppression of plastid division, and spontaneous light intensity-dependent localized cell death. A suppressor screen conducted on mutagenized crl mutants revealed that a missense mutation in OEP80 suppresses the pleiotropic defects of crl. Furthermore, we found that OEP80 complex formation is compromised in crl. Additionally, we demonstrated that CRL interacts with OEP80 in vivo and that a portion of CRL is present at the same molecular weight as the OEP80 complex. Our results suggest that CRL interacts with OEP80 to facilitate its complex formation. CRL is involved in plastid protein import; therefore, the pleiotropic defects in crl are likely due to the combined effects of decreased plastid protein import and altered membrane integration of β-barrel proteins in the outer envelope membrane. This study sheds light on the mechanisms that allow β-barrel protein integration into the plastid outer envelope membrane and the importance of this finding for plant cellular processes.
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