| アイテムタイプ |
itemtype_ver1(1) |
| 公開日 |
2024-05-23 |
| タイトル |
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タイトル |
CRUMPLED LEAF supports plastid OUTER ENVELOPE PROTEIN OF 80 KDA complex formation in Arabidopsis |
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言語 |
en |
| 著者 |
Yoshimura, Ryo
Minamikawa, Syun
Suzuki, Takamasa
Goto, Kotaro
Latrasse, David
Sicar, Sanchari
Raynaud, Cécile
Benhamed, Moussa
Yoshioka, Yasushi
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| アクセス権 |
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アクセス権 |
open access |
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アクセス権URI |
http://purl.org/coar/access_right/c_abf2 |
| 権利 |
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権利情報 |
This is a pre-copyedited, author-produced version of an article accepted for publication in [Plant Physiology] following peer review. The version of record [Ryo Yoshimura, Syun Minamikawa, Takamasa Suzuki, Kotaro Goto, David Latrasse, Sanchari Sicar, Cécile Raynaud, Moussa Benhamed, Yasushi Yoshioka, CRUMPLED LEAF supports plastid OUTER ENVELOPE PROTEIN OF 80 KDA complex formation in Arabidopsis, Plant Physiology, Volume 194, Issue 4, April 2024, Pages 2422–2433, https://doi.org/10.1093/plphys/kiae005] is available online at: https://doi.org/10.1093/plphys/kiae005. |
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言語 |
en |
| 内容記述 |
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内容記述タイプ |
Abstract |
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内容記述 |
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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言語 |
en |
| 出版者 |
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出版者 |
Oxford University Press |
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言語 |
en |
| 言語 |
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言語 |
eng |
| 資源タイプ |
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資源タイプresource |
http://purl.org/coar/resource_type/c_6501 |
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タイプ |
journal article |
| 出版タイプ |
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出版タイプ |
AM |
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出版タイプResource |
http://purl.org/coar/version/c_ab4af688f83e57aa |
| 関連情報 |
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関連タイプ |
isVersionOf |
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識別子タイプ |
DOI |
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関連識別子 |
https://doi.org/10.1093/plphys/kiae005 |
| 収録物識別子 |
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収録物識別子タイプ |
PISSN |
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収録物識別子 |
0032-0889 |
| 書誌情報 |
en : Plant Physiology
巻 194,
号 4,
p. 2422-2433,
発行日 2024-04
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| ファイル公開日 |
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日付 |
2025-04-01 |
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日付タイプ |
Available |
Ryo_Yoshimura_text.pdf (287 KB)
