YGL9 mediates LHC assembly by regulating LHCPs transport and chlorophyll synthesis in rice

SUMMARY LHC assembly is a fundamental process in forming a peripheral antenna system, which has a significant impact on photosynthesis. However, the molecular mechanism of the LHC assembly still needs to be further investigated in monocotyledonous plants. Here, we identified a bifunctional protein Y...

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Published inThe Plant journal : for cell and molecular biology Vol. 121; no. 3; pp. e17256 - n/a
Main Authors Zhang, Tianquan, Xiao, Wenwen, Wang, Zhongwei, Zhang, Jichao, Shen, Wenqiang, Tu, Ranran, Wu, Ruhui, Zhou, Kai, Sang, Xianchun, Ling, Yinghua, He, Guanghua, Zhang, Ting
Format Journal Article
LanguageEnglish
Published England 01.02.2025
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ISSN0960-7412
1365-313X
1365-313X
DOI10.1111/tpj.17256

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Abstract SUMMARY LHC assembly is a fundamental process in forming a peripheral antenna system, which has a significant impact on photosynthesis. However, the molecular mechanism of the LHC assembly still needs to be further investigated in monocotyledonous plants. Here, we identified a bifunctional protein YGL9 in rice, a homolog of cpSRP43 in Arabidopsis, mediates LHC assembly by simultaneously regulating LHCPs transport and chlorophyll synthesis. Mutation of YGL9 exhibits a yellow‐green leaf phenotype, with reduced LHCPs contents, impaired photosystem activity and reduced chlorophyll content. YGL9 interacts with cpSRP54 forming the cpSRP complex that transport LHCPs, and YGL9 also interacts with and stabilizes OsGUN4, which is an activator of MgCh and participates in the regulation of chlorophyll synthesis, to synergistically participate in chlorophyll synthesis. Further, genetic evidence demonstrates that YGL9 functions in the same pathway as cpSRP54 and OsGUN4 to regulate LHCPs transport and chlorophyll synthesis. Thus, our study reveals a cross‐relationship between LHCPs transport and chlorophyll synthesis, and provides new insights into the LHC assembly process in monocotyledonous plants. Significance Statement In this study, we identified a bifunctional protein YGL9 in rice, a homolog of cpSRP43 in Arabidopsis, which mediates LHC assembly by simultaneously regulating LHCPs transport and chlorophyll synthesis. Thus, our study reveals a cross‐relationship between LHCPs transport and chlorophyll synthesis and provides new insights into the LHC assembly process in monocotyledonous plants.
AbstractList LHC assembly is a fundamental process in forming a peripheral antenna system, which has a significant impact on photosynthesis. However, the molecular mechanism of the LHC assembly still needs to be further investigated in monocotyledonous plants. Here, we identified a bifunctional protein YGL9 in rice, a homolog of cpSRP43 in Arabidopsis, mediates LHC assembly by simultaneously regulating LHCPs transport and chlorophyll synthesis. Mutation of YGL9 exhibits a yellow-green leaf phenotype, with reduced LHCPs contents, impaired photosystem activity and reduced chlorophyll content. YGL9 interacts with cpSRP54 forming the cpSRP complex that transport LHCPs, and YGL9 also interacts with and stabilizes OsGUN4, which is an activator of MgCh and participates in the regulation of chlorophyll synthesis, to synergistically participate in chlorophyll synthesis. Further, genetic evidence demonstrates that YGL9 functions in the same pathway as cpSRP54 and OsGUN4 to regulate LHCPs transport and chlorophyll synthesis. Thus, our study reveals a cross-relationship between LHCPs transport and chlorophyll synthesis, and provides new insights into the LHC assembly process in monocotyledonous plants.LHC assembly is a fundamental process in forming a peripheral antenna system, which has a significant impact on photosynthesis. However, the molecular mechanism of the LHC assembly still needs to be further investigated in monocotyledonous plants. Here, we identified a bifunctional protein YGL9 in rice, a homolog of cpSRP43 in Arabidopsis, mediates LHC assembly by simultaneously regulating LHCPs transport and chlorophyll synthesis. Mutation of YGL9 exhibits a yellow-green leaf phenotype, with reduced LHCPs contents, impaired photosystem activity and reduced chlorophyll content. YGL9 interacts with cpSRP54 forming the cpSRP complex that transport LHCPs, and YGL9 also interacts with and stabilizes OsGUN4, which is an activator of MgCh and participates in the regulation of chlorophyll synthesis, to synergistically participate in chlorophyll synthesis. Further, genetic evidence demonstrates that YGL9 functions in the same pathway as cpSRP54 and OsGUN4 to regulate LHCPs transport and chlorophyll synthesis. Thus, our study reveals a cross-relationship between LHCPs transport and chlorophyll synthesis, and provides new insights into the LHC assembly process in monocotyledonous plants.
LHC assembly is a fundamental process in forming a peripheral antenna system, which has a significant impact on photosynthesis. However, the molecular mechanism of the LHC assembly still needs to be further investigated in monocotyledonous plants. Here, we identified a bifunctional protein YGL9 in rice, a homolog of cpSRP43 in Arabidopsis, mediates LHC assembly by simultaneously regulating LHCPs transport and chlorophyll synthesis. Mutation of YGL9 exhibits a yellow‐green leaf phenotype, with reduced LHCPs contents, impaired photosystem activity and reduced chlorophyll content. YGL9 interacts with cpSRP54 forming the cpSRP complex that transport LHCPs, and YGL9 also interacts with and stabilizes OsGUN4, which is an activator of MgCh and participates in the regulation of chlorophyll synthesis, to synergistically participate in chlorophyll synthesis. Further, genetic evidence demonstrates that YGL9 functions in the same pathway as cpSRP54 and OsGUN4 to regulate LHCPs transport and chlorophyll synthesis. Thus, our study reveals a cross‐relationship between LHCPs transport and chlorophyll synthesis, and provides new insights into the LHC assembly process in monocotyledonous plants.
SUMMARY LHC assembly is a fundamental process in forming a peripheral antenna system, which has a significant impact on photosynthesis. However, the molecular mechanism of the LHC assembly still needs to be further investigated in monocotyledonous plants. Here, we identified a bifunctional protein YGL9 in rice, a homolog of cpSRP43 in Arabidopsis, mediates LHC assembly by simultaneously regulating LHCPs transport and chlorophyll synthesis. Mutation of YGL9 exhibits a yellow‐green leaf phenotype, with reduced LHCPs contents, impaired photosystem activity and reduced chlorophyll content. YGL9 interacts with cpSRP54 forming the cpSRP complex that transport LHCPs, and YGL9 also interacts with and stabilizes OsGUN4, which is an activator of MgCh and participates in the regulation of chlorophyll synthesis, to synergistically participate in chlorophyll synthesis. Further, genetic evidence demonstrates that YGL9 functions in the same pathway as cpSRP54 and OsGUN4 to regulate LHCPs transport and chlorophyll synthesis. Thus, our study reveals a cross‐relationship between LHCPs transport and chlorophyll synthesis, and provides new insights into the LHC assembly process in monocotyledonous plants. Significance Statement In this study, we identified a bifunctional protein YGL9 in rice, a homolog of cpSRP43 in Arabidopsis, which mediates LHC assembly by simultaneously regulating LHCPs transport and chlorophyll synthesis. Thus, our study reveals a cross‐relationship between LHCPs transport and chlorophyll synthesis and provides new insights into the LHC assembly process in monocotyledonous plants.
LHC assembly is a fundamental process in forming a peripheral antenna system, which has a significant impact on photosynthesis. However, the molecular mechanism of the LHC assembly still needs to be further investigated in monocotyledonous plants. Here, we identified a bifunctional protein YGL9 in rice, a homolog of cpSRP43 in Arabidopsis , mediates LHC assembly by simultaneously regulating LHCPs transport and chlorophyll synthesis. Mutation of YGL9 exhibits a yellow‐green leaf phenotype, with reduced LHCPs contents, impaired photosystem activity and reduced chlorophyll content. YGL9 interacts with cpSRP54 forming the cpSRP complex that transport LHCPs, and YGL9 also interacts with and stabilizes OsGUN4, which is an activator of MgCh and participates in the regulation of chlorophyll synthesis, to synergistically participate in chlorophyll synthesis. Further, genetic evidence demonstrates that YGL9 functions in the same pathway as cpSRP54 and OsGUN4 to regulate LHCPs transport and chlorophyll synthesis. Thus, our study reveals a cross‐relationship between LHCPs transport and chlorophyll synthesis, and provides new insights into the LHC assembly process in monocotyledonous plants. In this study, we identified a bifunctional protein YGL9 in rice, a homolog of cpSRP43 in Arabidopsis, which mediates LHC assembly by simultaneously regulating LHCPs transport and chlorophyll synthesis. Thus, our study reveals a cross‐relationship between LHCPs transport and chlorophyll synthesis and provides new insights into the LHC assembly process in monocotyledonous plants.
Author Zhang, Tianquan
Zhang, Jichao
Shen, Wenqiang
Xiao, Wenwen
Ling, Yinghua
Zhang, Ting
Zhou, Kai
Wu, Ruhui
He, Guanghua
Tu, Ranran
Sang, Xianchun
Wang, Zhongwei
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  organization: Southwest University
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Snippet SUMMARY LHC assembly is a fundamental process in forming a peripheral antenna system, which has a significant impact on photosynthesis. However, the molecular...
LHC assembly is a fundamental process in forming a peripheral antenna system, which has a significant impact on photosynthesis. However, the molecular...
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StartPage e17256
SubjectTerms Arabidopsis
Biological Transport
chlorophyll
Chlorophyll - biosynthesis
Chlorophyll - metabolism
Gene Expression Regulation, Plant
leaves
Light-Harvesting Protein Complexes - genetics
Light-Harvesting Protein Complexes - metabolism
mutation
Oryza - genetics
Oryza - metabolism
phenotype
Photosynthesis
Plant Proteins - genetics
Plant Proteins - metabolism
rice
Title YGL9 mediates LHC assembly by regulating LHCPs transport and chlorophyll synthesis in rice
URI https://onlinelibrary.wiley.com/doi/abs/10.1111%2Ftpj.17256
https://www.ncbi.nlm.nih.gov/pubmed/39932448
https://www.proquest.com/docview/3165414616
https://www.proquest.com/docview/3200265838
Volume 121
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