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Oil bodies' proteins - Arabidopsis thaliana

ABSTRACT: Oil bodies' proteins identified after SDS-PAGE (18kDa band) and chymotrypsin digestion.

INSTRUMENT(S): LCQ Deca, instrument model

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

SUBMITTER: Martina Vermachova

PROVIDER: PRD000392 | Pride | 2011-09-28

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	PRIDE_Exp_Complete_Ac_16506.pride.mgf.gz	Mgf
	PRIDE_Exp_Complete_Ac_16506.pride.mztab.gz	Mztab
	PRIDE_Exp_Complete_Ac_16506.xml.gz	Xml
	PRIDE_Exp_Complete_Ac_16507.pride.mgf.gz	Mgf
	PRIDE_Exp_Complete_Ac_16507.pride.mztab.gz	Mztab

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Publications

New protein isoforms identified within Arabidopsis thaliana seed oil bodies combining chymotrypsin/trypsin digestion and peptide fragmentation analysis.

Vermachova Martina M Purkrtova Zita Z Santrucek Jiri J Jolivet Pascale P Chardot Thierry T Kodicek Milan M

Proteomics 20110801 16

Plant seed oil bodies, subcellular lipoprotein inclusions providing storage reserves, are composed of a neutral lipid core surrounded by a phospholipid monolayer with several integrated proteins that play a significant role in stabilization of the particles and probably also in lipid mobilization. Oil bodies' proteins are generally very hydrophobic, due to the long uncharged sequences anchoring them into the lipid core, which makes them extremely difficult to handle and to digest successfully. A ...[more]

PMID: 21751352

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Oil body - LC-MS/MS methods for absolute quantification and identification of proteins associated with chimeric plant oil bodies

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Membrane Fraction Complexome of Nitrososphaera viennensis with BN-PAGE and Examination of the Archaeal Ammonia Monooxygenase Complex via SDS-Tricine-PAGE

Project description:Information on the files related to the respective experiments can be found in the metadata file titled “Metadata_for_Nviennensis_Experiments.xlsx”. The data found here encompasses three related mass spectrometry experiments: 1.) BN-PAGE: Biomass of Nitrososphaera viennensis grown in a bioreactor was lysed and membrane fractions were harvested using an ultracentrifuge. Membrane proteins were extracted using n-dodecyl-beta-D-maltoside (DDM) and loaded on a 3-12% gradient blue native PAGE gel. Selected bands were cut out and analyzed via mass spectrometry. 2.) SDS-Tricine-PAGE of AMO Band: A band containing a large amount of the ammonia monooxygenase complex (AMO) was denatured and run on a 15% SDS-Tricine-PAGE gel to identify individual subunits. 3.) AmoC from SDS-Tricine-PAGE: A band containing a high amount of AmoC from the SDS-Tricine-PAGE gel was processed with three separate digestive enzymes (trypsin, chymotrypsin, or GluC) to identify unique peptides among the six AmoC homologs found in the genome of N. viennensis.

2023-02-13 | PXD035349 | Pride

ALGOMICS - Proteomic profiling of oil bodies isolated from the unicellular green microalga Chlamydomonas reinhardtii: with focus on proteins involved in lipid metabolism

Project description:Oil-bodies are sites of energy storage in many organisms including microalgae. As a first step toward understanding oil accumulation in algae, we took a proteomic approach on purified oil-body fraction from the model microalga Chlamydomonas reinhardtii grown under nitrogen deprivation. Among the 240 proteins (?2 peptides) identified by LC-MS/MS, 33 were putatively involved in metabolism of lipids (mostly acyl-lipids and sterols). Compared to a recently reported Chlamydomonas oil-body proteome, 19 additional proteins of lipid metabolism were identified, including a glycerol 3-phosphate acyltransferase (GPAT), a lysophosphatidic acid acyltransferase (LPAT) and a putative phospholipid:diacylglycerol acyltransferase (PDAT), spanning the key steps of the triacylglycerol synthesis pathway. In addition, proteins putatively involved in deacylation/reacylation, sterol synthesis, lipid signaling and lipid trafficking were found to be associated to the oil body fraction. This dataset thus provides evidence that in Chlamydomonas oil-bodies are not only storage compartments but also are dynamic structures likely to be involved in processes such as oil synthesis, degradation and lipid homeostasis. The proteins identified here should provide useful targets for genetic studies aiming at increasing our understanding of triacyglycerol synthesis and the role of oil-bodies in microalgal cell functions.

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Arabidopsis thaliana comparative leaf proteomics of Clp protease mutant

Project description:Arabidopsis total leaf proteomics p3mutant biol replicate1 SDS-PAGE Band10, in-gel trypsin digestion LTQ Orbitrap

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Sucrose Production Mediated by Lipid Metabolism Suppresses the Physical Interaction of Peroxisomes and Oil Bodies during Germination of Arabidopsis thaliana.

Project description:Physical interaction between organelles is a flexible event and essential for cells to adapt rapidly to environmental stimuli. Germinating plants utilize oil bodies and peroxisomes to mobilize storage lipids for the generation of sucrose as the main energy source. Although membrane interaction between oil bodies and peroxisomes has been widely observed, its underlying molecular mechanism is largely unknown. Here we present genetic evidence for control of the physical interaction between oil bodies and peroxisomes. We identified alleles of the sdp1 mutant altered in oil body morphology. This mutant accumulates bigger and more oil body aggregates compared with the wild type and showed defects in lipid mobilization during germination. SUGAR DEPENDENT 1 (SDP1) encodes major triacylglycerol lipase in Arabidopsis Interestingly, sdp1 seedlings show enhanced physical interaction between oil bodies and peroxisomes compared with the wild type, whereas exogenous sucrose supplementation greatly suppresses the interaction. The same phenomenon occurs in the peroxisomal defective 1 (ped1) mutant, defective in lipid mobilization because of impaired peroxisomal β-oxidation, indicating that sucrose production is a key factor for oil body-peroxisomal dissociation. Peroxisomal dissociation and subsequent release from oil bodies is dependent on actin filaments. We also show that a peroxisomal ATP binding cassette transporter, PED3, is the potential anchor protein to the membranes of these organelles. Our results provide novel components linking lipid metabolism and oil body-peroxisome interaction whereby sucrose may act as a negative signal for the interaction of oil bodies and peroxisomes to fine-tune lipolysis.

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Arabidopsis thaliana

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Peroxisome extensions deliver the Arabidopsis SDP1 lipase to oil bodies.

Project description:Lipid droplets/oil bodies (OBs) are lipid-storage organelles that play a crucial role as an energy resource in a variety of eukaryotic cells. Lipid stores are mobilized in the case of food deprivation or high energy demands--for example, during certain developmental processes in animals and plants. OB degradation is achieved by lipases that hydrolyze triacylglycerols (TAGs) into free fatty acids and glycerol. In the model plant Arabidopsis thaliana, Sugar-Dependent 1 (SDP1) was identified as the major TAG lipase involved in lipid reserve mobilization during seedling establishment. Although the enzymatic activity of SDP1 is associated with the membrane of OBs, its targeting to the OB surface remains uncharacterized. Here we demonstrate that the core retromer, a complex involved in protein trafficking, participates in OB biogenesis, lipid store degradation, and SDP1 localization to OBs. We also report an as-yet-undescribed mechanism for lipase transport in eukaryotic cells, with SDP1 being first localized to the peroxisome membrane at early stages of seedling growth and then possibly moving to the OB surface through peroxisome tubulations. Finally, we show that the timely transfer of SDP1 to the OB membrane requires a functional core retromer. In addition to revealing previously unidentified functions of the retromer complex in plant cells, our work provides unanticipated evidence for the role of peroxisome dynamics in interorganelle communication and protein transport.

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