Arabidopsis Sec14 proteins (SFH5 and SFH7) mediate interorganelle transport of phosphatidic acid and regulate chloroplast development.
Arabidopsis Sec14 proteins (SFH5 and SFH7) mediate interorganelle transport of phosphatidic acid and regulate chloroplast development.
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拟南芥 Sec14 蛋白(SFH5 和 SFH7)介导磷脂酸的细胞器间转运并调节叶绿体发育
DOI:
10.1073/pnas.2221637120
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发表时间:
2023-02-07
影响因子:
11.1
通讯作者:
Xue, Hong -Wei
中科院分区:
文献类型:
--
作者:
Yao, Hong-Yan;Lu, Yao-Qi;Yang, Xiao-Li;Wang, Xiao-Qing;Luo, Zhipu;Lin, De -Li;Wu, Jia-Wei;Xue, Hong -Wei
Solar is converted to chemical energy at thylakoid membranes of eukaryotic photosynthetic organisms, and proper lipid assembly in thylakoid membrane, particularly the transfer of lipid precursors from other organelles, is crucial. Sec14 homology proteins are identified in all eukaryotes, which can bind and transfer a wide range of lipids. By crystallizing the Sec14 domain of Arabidopsis Sec14 homology protein5 (AtSFH5) and relevant biochemical and genetic studies, we elucidated the specific binding modes of phosphatidic acid (PA) and unique structural features of plant Sec14 domains, and demonstrated the crucial roles of AtSFH5 and AtSFH7 in regulating chloroplast development providing a model for interorganelle phospholipid transport and a mechanism involving in the adaptive evolution of cellular plastids. Lipids establish the specialized thylakoid membrane of chloroplast in eukaryotic photosynthetic organisms, while the molecular basis of lipid transfer from other organelles to chloroplast remains further elucidation. Here we revealed the structural basis of Arabidopsis Sec14 homology proteins AtSFH5 and AtSFH7 in transferring phosphatidic acid (PA) from endoplasmic reticulum (ER) to chloroplast, and whose function in regulating the lipid composition of chloroplast and thylakoid development. AtSFH5 and AtSFH7 localize at both ER and chloroplast, whose deficiency resulted in an abnormal chloroplast structure and a decreased thickness of stacked thylakoid membranes. We demonstrated that AtSFH5, but not yeast and human Sec14 proteins, could specifically recognize and transfer PA in vitro. Crystal structures of the AtSFH5-Sec14 domain in complex with L-α-phosphatidic acid (L-α-PA) and 1,2-dipalmitoyl-sn-glycero-3-phosphate (DPPA) revealed that two PA ligands nestled in the central cavity with different configurations, elucidating the specific binding mode of PA to AtSFH5, different from the reported phosphatidylethanolamine (PE)/phosphatidylcholine (PC)/phosphatidylinositol (PI) binding modes. Quantitative lipidomic analysis of chloroplast lipids showed that PA and monogalactosyldiacylglycerol (MGDG), particularly the C18 fatty acids at sn-2 position in MGDG were significantly decreased, indicating a disrupted ER-to-plastid (chloroplast) lipid transfer, under deficiency of AtSFH5 and AtSFH7. Our studies identified the role and elucidated the structural basis of plant SFH proteins in transferring PA between organelles, and suggested a model for ER-chloroplast interorganelle phospholipid transport from inherent ER to chloroplast derived from endosymbiosis of a cyanobacteriumproviding a mechanism involved in the adaptive evolution of cellular plastids.
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DOI:
10.1073/pnas.100132197
发表时间:
2000-07-05
影响因子:
11.1
作者:
Jarvis, P;Dörmann, P;Chory, J
通讯作者:
Chory, J
DOI:
10.1073/pnas.1609184113
发表时间:
2016-09-20
影响因子:
11.1
作者:
Kelly, Amelie A.;Kalisch, Barbara;Doermann, Peter
通讯作者:
Doermann, Peter
影响因子:
3.3
作者:
Ghosh R;de Campos MK;Huang J;Huh SK;Orlowski A;Yang Y;Tripathi A;Nile A;Lee HC;Dynowski M;Schäfer H;Róg T;Lete MG;Ahyayauch H;Alonso A;Vattulainen I;Igumenova TI;Schaaf G;Bankaitis VA
通讯作者:
Bankaitis VA
影响因子:
56.9
作者:
Dörmann, P;Balbo, I;Benning, C
通讯作者:
Benning, C
DOI:
10.1107/s0907444904019158
发表时间:
2004-12-01
影响因子:
2.2
作者:
Emsley, P;Cowtan, K
通讯作者:
Cowtan, K