气候变化领域集成服务门户(CCPortal): A Sec14 domain protein is required for photoautotrophic growth and chloroplast vesicle formation in Arabidopsis thaliana

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DOI	10.1073/pnas.1916946117
	A Sec14 domain protein is required for photoautotrophic growth and chloroplast vesicle formation in Arabidopsis thaliana
	Hertle A.P.; García-Cerdán J.G.; Armbruster U.; Shih R.; Lee J.J.; Wong W.; Niyogi K.K.
发表日期	2020
ISSN	0027-8424
起始页码	9101
结束页码	9111
卷号	117 期号:16
英文摘要	In eukaryotic photosynthetic organisms, the conversion of solar into chemical energy occurs in thylakoid membranes in the chloroplast. How thylakoid membranes are formed and maintained is poorly understood. However, previous observations of vesicles adjacent to the stromal side of the inner envelope membrane of the chloroplast suggest a possible role of membrane transport via vesicle trafficking from the inner envelope to the thylakoids. Here we show that the model plant Arabidopsis thaliana has a chloroplast-localized Sec14-like protein (CPSFL1) that is necessary for photoautotrophic growth and vesicle formation at the inner envelope membrane of the chloroplast. The cpsfl1 mutants are seedling lethal, show a defect in thylakoid structure, and lack chloroplast vesicles. Sec14 domain proteins are found only in eukaryotes and have been well characterized in yeast, where they regulate vesicle budding at the trans-Golgi network. Like the yeast Sec14p, CPSFL1 binds phosphatidylinositol phosphates (PIPs) and phosphatidic acid (PA) and acts as a phosphatidylinositol transfer protein in vitro, and expression of Arabidopsis CPSFL1 can complement the yeast sec14 mutation. CPSFL1 can transfer PIP into PA-rich membrane bilayers in vitro, suggesting that CPSFL1 potentially facilitates vesicle formation by trafficking PA and/or PIP, known regulators of membrane trafficking between organellar subcompartments. These results underscore the role of vesicles in thylakoid biogenesis and/or maintenance. CPSFL1 appears to be an example of a eukaryotic cytosolic protein that has been coopted for a function in the chloroplast, an organelle derived from endosymbiosis of a cyanobacterium. © 2020 National Academy of Sciences. All rights reserved.
英文关键词	Chloroplast; CRAL_TRIO domain; Phosphoinositides; Sec14 domain; Thylakoid biogenesis
语种	英语
scopus关键词	chloroplast localized Sec14 liek protein; mutant protein; phosphatidic acid; phosphatidylinositol; plant protein; polyphosphoinositide; Sec14 domain protein; unclassified drug; Arabidopsis protein; phospholipid transfer protein; recombinant protein; Saccharomyces cerevisiae protein; SEC14 protein, S cerevisiae; Arabidopsis thaliana; Article; budding yeast; cell compartmentalization; cell nucleus membrane; cell organelle; cell structure; cell vacuole; cellular distribution; chloroplast; controlled study; cpsfl1 gene; cyanobacterium; endosymbiosis; eukaryote; gene mutation; in vitro study; lipid bilayer; nonhuman; photoautotrophic growth; plant growth; plastid; priority journal; protein binding; protein expression; protein function; protein transport; sec14 gene; seedling; seedling lethal; thylakoid; trans Golgi network; ultrastructure; yeast; Arabidopsis; genetics; metabolism; mutation; photosynthesis; physiology; protein domain; Saccharomyces cerevisiae; sequence homology; transgenic plant; transmission electron microscopy; Arabidopsis; Arabidopsis Proteins; Microscopy, Electron, Transmission; Mutation; Phosphatidic Acids; Phosphatidylinositol Phosphates; Phospholipid Transfer Proteins; Photosynthesis; Plants, Genetically Modified; Protein Domains; Recombinant Proteins; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Seedlings; Sequence Homology, Amino Acid; Thylakoids
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/160301
作者单位	Hertle, A.P., Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, United States, Department of Organelle Biology, Biotechnology, and Molecular Eco-physiology, Max Planck Institute of Molecular Plant Physiology, Potsdam-Golm, D-14476, Germany; García-Cerdán, J.G., Department of Plant and Microbial Biology, University of California, Berkeley, CA 94720-3102, United States, Howard Hughes Medical Institute, University of California, Berkeley, CA 94720, United States; Armbruster, U., Department of Plant and Microbial Biology, University of California, Berkeley, CA 94720-3102, United States, Department of Organelle Biology, Biotechnology, and Molecular Eco-physiology, Max Planck Institute of Molecular Plant Physiology, Potsdam-Golm, D-14476, Germany; Shih, R., Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, United States; Lee, J.J., Department of Plant and Microbial Biology, Un...
推荐引用方式 GB/T 7714	Hertle A.P.,García-Cerdán J.G.,Armbruster U.,et al. A Sec14 domain protein is required for photoautotrophic growth and chloroplast vesicle formation in Arabidopsis thaliana[J],2020,117(16).
APA	Hertle A.P..,García-Cerdán J.G..,Armbruster U..,Shih R..,Lee J.J..,...&Niyogi K.K..(2020).A Sec14 domain protein is required for photoautotrophic growth and chloroplast vesicle formation in Arabidopsis thaliana.Proceedings of the National Academy of Sciences of the United States of America,117(16).
MLA	Hertle A.P.,et al."A Sec14 domain protein is required for photoautotrophic growth and chloroplast vesicle formation in Arabidopsis thaliana".Proceedings of the National Academy of Sciences of the United States of America 117.16(2020).