New Functions of the Thylakoid Membrane Proteome of Arabidopsis thaliana Revealed by a Simple, Fast, and Versatile Fractionation Strategy

Peltier, Jean‐Benoǐt; Ytterberg, A. Jimmy; Sun, Qi; Wijk, Klaas J. van

doi:10.1074/jbc.m406763200

Cited by 250 publications

(212 citation statements)

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“…Pepper homologs were identified for two of those (At1g32220 and At4g13200; Table III). Three of them (At4g13200, At4g01150, and At3g10130) were also identified in our earlier studies on the hydrophobic thylakoid proteome (Friso et al, 2004;Peltier et al, 2004). At4g01150 showed a 3-fold increased relative accumulation in PGs after HL.…”

Section: Other Proteinsmentioning

confidence: 95%

“…Most of the proteins were never identified in the stromal or envelope proteome, clearly indicating that PGs contain a specific protein population (Table I). A number of proteins were identified during our previous in-depth analyses of the thylakoid membranes (Friso et al, 2004;Peltier et al, 2004), which is not surprising because PGs are associated with the thylakoid membrane (Table I). Only one (At4g01150) of the 33 PG proteins has predicted transmembrane domains.…”

Section: Purification Identification and Comparison Of Pg Proteomesmentioning

confidence: 99%

“…For rice proteome data, we searched the OsGi database downloaded from The Institute for Genomic Research (TIGR; http://www.tigr.org). Criteria for positive identification from peptide mass fingerprinting are described by Friso et al (2004) and for MS/MS data by Peltier et al (2004). Identified proteins without unique peptides (i.e.…”

Section: Protein Identification By Msmentioning

confidence: 99%

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Protein Profiling of Plastoglobules in Chloroplasts and Chromoplasts. A Surprising Site for Differential Accumulation of Metabolic Enzymes

2006

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Plastoglobules (PGs) are oval or tubular lipid-rich structures present in all plastid types, but their specific functions are unclear. PGs contain quinones, a-tocopherol, and lipids and, in chromoplasts, carotenoids as well. It is not known whether PGs contain any enzymes or regulatory proteins. Here, we determined the proteome of PGs from chloroplasts of stressed and unstressed leaves of Arabidopsis (Arabidopsis thaliana) as well as from pepper (Capsicum annuum) fruit chromoplasts using mass spectrometry. Together, this showed that the proteome of chloroplast PGs consists of seven fibrillins, providing a protein coat and preventing coalescence of the PGs, and an additional 25 proteins likely involved in metabolism of isoprenoid-derived molecules (quinines and tocochromanols), lipids, and carotenoid cleavage. Four unknown ABC1 kinases were identified, possibly involved in regulation of quinone monooxygenases. Most proteins have not been observed earlier but have predicted N-terminal chloroplast transit peptides and lack transmembrane domains, consistent with localization in the PG lipid monolayer particles. Quantitative differences in PG composition in response to high light stress and degreening were determined by differential stable-isotope labeling using formaldehyde. More than 20 proteins were identified in the PG proteome of pepper chromoplasts, including four enzymes of carotenoid biosynthesis and several homologs of proteins observed in the chloroplast PGs. Our data strongly suggest that PGs in chloroplasts form a functional metabolic link between the inner envelope and thylakoid membranes and play a role in breakdown of carotenoids and oxidative stress defense, whereas PGs in chromoplasts are also an active site for carotenoid conversions.

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Section: Other Proteinsmentioning

confidence: 95%

Section: Purification Identification and Comparison Of Pg Proteomesmentioning

confidence: 99%

Section: Protein Identification By Msmentioning

confidence: 99%

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Protein Profiling of Plastoglobules in Chloroplasts and Chromoplasts. A Surprising Site for Differential Accumulation of Metabolic Enzymes

2006

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“…In recent years, proteomic studies of the chloroplastic envelope membrane (Ferro et al, 2003;Froehlich et al, 2003), thylakoid membrane (Friso et al, 2004;Peltier et al, 2004), and luminal fraction (Peltier et al, 2002;Schubert et al, 2002;Goulas et al, 2006) have provided clearer knowledge of the chloroplastic proteome of Arabidopsis (Arabidopsis thaliana). The most abundant protein complexes, such as PSII and PSI, cytochrome b 6 f, and ATP synthase, are photosynthetic apparatuses located at the thylakoid membrane for biogenesis.…”

mentioning

confidence: 99%

Structural and Functional Assays of AtTLP18.3 Identify Its Novel Acid Phosphatase Activity in Thylakoid Lumen

Liu

Lin

et al. 2011

Plant Physiology

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The membrane protein AtTLP18.3 of Arabidopsis (Arabidopsis thaliana) contains a domain of unknown function, DUF477; it forms a polysome with photosynthetic apparatuses in the thylakoid lumen. To explore the molecular function of AtTLP18.3, we resolved its crystal structures with residues 83 to 260, the DUF477 only, and performed a series of biochemical analyses to discover its function. The gene expression of AtTLP18.3 followed a circadian rhythm. X-ray crystallography revealed the folding of AtTLP18.3 as a three-layer sandwich with three a-helices in the upper layer, four b-sheets in the middle layer, and two a-helices in the lower layer, which resembles a Rossmann fold. Structural comparison suggested that AtTLP18.3 might be a phosphatase. The enzymatic activity of AtTLP18.3 was further confirmed by phosphatase assay with various substrates (e.g. p-nitrophenyl phosphate, 6,8-difluoro-4-methylumbelliferyl phosphate, O-phospho-L-serine, and several synthetic phosphopeptides). Furthermore, we obtained the structure of AtTLP18.3 in complex with O-phospho-L-serine to identify the binding site of AtTLP18.3. Our structural and biochemical studies revealed that AtTLP18.3 has the molecular function of a novel acid phosphatase in the thylakoid lumen. DUF477 is accordingly renamed the thylakoid acid phosphatase domain.

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“…THF1 has also been implicated in the response to coronatine (COR) during the interaction between tomato and Pseudomonas syringae (Wangdi et al, 2010). THF1 has been reported to have a complex organellar distribution, being detected in the envelope, thylakoid membrane, and stroma of Arabidopsis chloroplasts (Peltier et al, 2004(Peltier et al, , 2006. However, coimmunoprecipitation (Co-IP) and bimolecular fluorescence complementation (BIFC) experiments indicated that THF1 and I2-like CC domains interact in the cytosol.…”

mentioning

confidence: 99%

The Chloroplastic Protein THF1 Interacts with the Coiled-Coil Domain of the Disease Resistance Protein N′ and Regulates Light-Dependent Cell Death

et al. 2016

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One branch of plant immunity is mediated through nucleotide-binding/Leu-rich repeat (NB-LRR) family proteins that recognize specific effectors encoded by pathogens. Members of the I2-like family constitute a well-conserved subgroup of NB-LRRs from Solanaceae possessing a coiled-coil (CC) domain at their N termini. We show here that the CC domains of several I2-like proteins are able to induce a hypersensitive response (HR), a form of programmed cell death associated with disease resistance. Using yeast two-hybrid screens, we identified the chloroplastic protein Thylakoid Formation1 (THF1) as an interacting partner for several I2-like CC domains. Co-immunoprecipitations and bimolecular fluorescence complementation assays confirmed that THF1 and I2-like CC domains interact in planta and that these interactions take place in the cytosol. Several HR-inducing I2-like CC domains have a negative effect on the accumulation of THF1, suggesting that the latter is destabilized by active CC domains. To confirm this model, we investigated N9, which recognizes the coat protein of most Tobamoviruses, as a prototypical member of the I2-like family. Transient expression and gene silencing data indicated that THF1 functions as a negative regulator of cell death and that activation of full-length N9 results in the destabilization of THF1. Consistent with the known function of THF1 in maintaining chloroplast homeostasis, we show that the HR induced by N9 is light-dependent. Together, our results define, to our knowledge, novel molecular mechanisms linking light and chloroplasts to the induction of cell death by a subgroup of NB-LRR proteins.

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New Functions of the Thylakoid Membrane Proteome of Arabidopsis thaliana Revealed by a Simple, Fast, and Versatile Fractionation Strategy

Cited by 250 publications

References 87 publications

Protein Profiling of Plastoglobules in Chloroplasts and Chromoplasts. A Surprising Site for Differential Accumulation of Metabolic Enzymes

Protein Profiling of Plastoglobules in Chloroplasts and Chromoplasts. A Surprising Site for Differential Accumulation of Metabolic Enzymes

Structural and Functional Assays of AtTLP18.3 Identify Its Novel Acid Phosphatase Activity in Thylakoid Lumen

The Chloroplastic Protein THF1 Interacts with the Coiled-Coil Domain of the Disease Resistance Protein N′ and Regulates Light-Dependent Cell Death

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