Chloroplast vesicle transport

Lindquist, Emelie; Aronsson, Henrik

doi:10.1007/s11120-018-0566-0

Cited by 26 publications

(23 citation statements)

References 97 publications

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“…By contrast, the Bienertia chloroplast has an elaborate thylakoid network in the stroma and the construction process is confined to the vicinity of the envelope membrane (within 100 nm from IEM). Given that we did not identify vesicle-like carriers in the stroma, roles of vesicle carriers reported earlier from studies in higher plants 28 seems limited in the Bienertia thylakoid assembly.…”

Section: Discussioncontrasting

confidence: 55%

Electron Tomography Analysis of Thylakoid Assembly and Fission in Chloroplasts of a Single-Cell C4 plant, Bienertia sinuspersici

Yeung

Han

et al. 2019

Sci Rep

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Bienertia sinuspersici is a single-cell C4 plant species of which chlorenchyma cells have two distinct groups of chloroplasts spatially segregated in the cytoplasm. The central vacuole encloses most chloroplasts at the cell center and confines the rest of the chloroplasts near the plasma membrane. Young chlorenchyma cells, however, do not have large vacuoles and their chloroplasts are homogenous. Therefore, maturing Bienertia chlorenchyma cells provide a unique opportunity to investigate chloroplast proliferation in the central cluster and the remodeling of chloroplasts that have been displaced by the vacuole to the cell periphery. Chloroplast numbers and sizes increased, more notably, during later stages of maturation than the early stages. Electron tomography analyses indicated that chloroplast enlargement is sustained by thylakoid growth and that invaginations from the inner envelope membrane contributed to thylakoid assembly. Grana stacks acquired more layers, differentiating them from stroma thylakoids as central chloroplasts matured. In peripheral chloroplasts, however, grana stacks stretched out to a degree that the distinction between grana stacks and stroma thylakoids was obscured. In central chloroplasts undergoing division, thylakoids inside the cleavage furrow were kinked and severed. Grana stacks in the division zone were disrupted, and large complexes in their membranes were dislocated, suggesting the existence of a thylakoid fission machinery.

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Section: Discussioncontrasting

confidence: 55%

Electron Tomography Analysis of Thylakoid Assembly and Fission in Chloroplasts of a Single-Cell C4 plant, Bienertia sinuspersici

Yeung

Han

et al. 2019

Sci Rep

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“…Putative components involved in chloroplast vesicle trafficking have been identified by previous genetic studies in Arabidopsis (52)(53)(54). Mutants such as fzl (25), thf1 (26), cprabA5e (23), and sco2 (24) were shown to accumulate chloroplast vesicles, whereas vipp1 mutants have been reported to lack chloroplast vesicles (4), similar to cpsfl1.…”

Section: Discussionmentioning

confidence: 99%

A Sec14 domain protein is required for photoautotrophic growth and chloroplast vesicle formation in Arabidopsis thaliana

Hertle

García-Cerdán

Armbruster

et al. 2020

Proc. Natl. Acad. Sci. U.S.A.

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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.

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“…While diverse functions have been attributed to IM30 in the past 1,2,[10][11][12][13][14][15][16][17][18][19][20][21][22][23][24] , most observations clearly indicate that the protein is membrane-active and involved in the biogenesis, dynamics and/or stabilization of internal membranes in chloroplasts and cyanobacteria (recently reviewed in 25 ). Thus, the physiological function of IM30 appears to be linked to dynamic membrane remodeling [25][26][27] , likely involving membrane fusion/fission events, which have been observed in plant chloroplasts [28][29][30][31] . In fact, dynamic rearrangement of the TM system is crucial for adaptation of photosynthetic processes to altering environmental conditions, most importantly in response to altering light intensities 32,33 .…”

mentioning

confidence: 99%

GTP hydrolysis by Synechocystis IM30 does not decisively affect its membrane remodeling activity

Junglas

Siebenaller

Schlösser

et al. 2020

Sci Rep

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The function of IM30 (also known as Vipp1) is linked to protection and/or remodeling of the thylakoid membrane system in chloroplasts and cyanobacteria. Recently, it has been revealed that the Arabidopsis IM30 protein exhibits GTP hydrolyzing activity in vitro, which was unexpected, as IM30 does not show any classical GTPase features. In the present study, we addressed the question, whether an apparent GTPase activity is conserved in IM30 proteins and can also be observed for IM30 of the cyanobacterium Synechocystis sp. PCC 6803. We show that Synechocystis IM30 is indeed able to bind and hydrolyze GTP followed by the release of P i. Yet, the apparent GTPase activity of Synechocystis IM30 does not depend on Mg 2+ , which, together with the lack of classical GTPase features, renders IM30 an atypical GTPase. To elucidate the impact of this cryptic GTPase activity on the membrane remodeling activity of IM30, we tested whether GTP hydrolysis influences IM30 membrane binding and/or IM30mediated membrane fusion. We show that membrane remodeling by Synechocystis IM30 is slightly affected by nucleotides. Yet, despite IM30 clearly catalyzing GTP hydrolysis, this does not seem to be vital for its membrane remodeling function.

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Chloroplast vesicle transport

Cited by 26 publications

References 97 publications

Electron Tomography Analysis of Thylakoid Assembly and Fission in Chloroplasts of a Single-Cell C4 plant, Bienertia sinuspersici

Electron Tomography Analysis of Thylakoid Assembly and Fission in Chloroplasts of a Single-Cell C4 plant, Bienertia sinuspersici

A Sec14 domain protein is required for photoautotrophic growth and chloroplast vesicle formation in Arabidopsis thaliana

GTP hydrolysis by Synechocystis IM30 does not decisively affect its membrane remodeling activity

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