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Seedling proteome of Arabidopsis thaliana pux10-3 mutant

ABSTRACT: description: Lipid droplets (LD) of seedlings lacking PUX10 stay significantly smaller during germination than the LDs of wild type seedlings. The observation that the removal of a LD-associated protein from a plant affects LD morphology has been observed previously {Siloto et al., 2006}{Gidda et al., 2016}. Especially the effect of the knock-out of the major structural LD protein Oleosin1 leading to a strongly increased size of LDs described by Siloto et al. might indicate that the abundance of structural LD proteins influences the LD size. Thus, the influence of the absence of PUX10 on the abundance of these proteins was investigated via a proteomic approach. Here, proteins isolated from homogenized seedlings of different lines (Ws-4 and pux10-3) and different developmental stages (wet seeds, and 1 to 3 days after imbibition (dai)) were subjected to tryptic digest and LC-MS/MS analysis.

INSTRUMENT(S): LTQ Orbitrap Velos

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

TISSUE(S): Seedling

SUBMITTER: Till Ischebeck

LAB HEAD: Dr. Till Ischebeck

PROVIDER: PXD009397 | Pride | 2018-08-13

REPOSITORIES: Pride

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			Action	DRS
	0daipeptides.txt	Txt
	0daiproteinGroups.txt	Txt
	1daipeptides.txt	Txt
	1daiproteinGroups.txt	Txt
	2daipeptides.txt	Txt

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Seedling proteome of Arabidopsis thaliana pux10-1 mutants

Project description:Lipid droplets (LD) of seedlings lacking PUX10 stay significantly smaller during germination than the LDs of wild type seedlings. The observation that the removal of a LD-associated protein from a plant affects LD morphology has been observed previously {Siloto et al., 2006}{Gidda et al., 2016}. Especially the effect of the knock-out of the major structural LD protein Oleosin1 leading to a strongly increased size of LDs described by Siloto et al. might indicate that the abundance of structural LD proteins influences the LD size. Thus, the influence of the absence of PUX10 on the abundance of these proteins was investigated via a proteomic approach. Here, proteins isolated from homogenized seedlings of different lines (qrt PUX10, qrt pux10-1, complemented 1, and complemented 2) and different developmental stages (wet seeds, and 1 to 3 days after imbibition (dai)) were subjected to tryptic digest and LC-MS/MS analysis.

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Seedling proteome of Arabidopsis thaliana pux10-3 mutants

Project description:Lipid droplets (LD) of seedlings lacking PUX10 stay significantly smaller during germination than the LDs of wild type seedlings. The observation that the removal of a LD-associated protein from a plant affects LD morphology has been observed previously {Siloto et al., 2006}{Gidda et al., 2016}. Especially the effect of the knock-out of the major structural LD protein Oleosin1 leading to a strongly increased size of LDs described by Siloto et al. might indicate that the abundance of structural LD proteins influences the LD size. Thus, the influence of the absence of PUX10 on the abundance of these proteins was investigated via a proteomic approach. Here, proteins isolated from homogenized seedlings of different lines (Ws-4 and pux10-3) and different developmental stages (wet seeds, and 1 to 3 days after imbibition (dai)) were subjected to tryptic digest and LC-MS/MS analysis.

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Proteome of Arabidopsis thaliana pux10-1 mutant lipid droplets

Project description:The analysis of proteins isolated from whole seedling homogenate allowed insight into the abundance of lipid droplet proteins in different lines and time points. In order to gain more detailed insight into the protein composition of LDs of the different mutant lines and to increase the chances for the detection of post-translationally modified peptides, LD-enriched fractions were analyzed in a second proteomic approach. The LD fraction was isolated from homogenized seedlings of qrt PUX10, qrt pux10-1, C#1, and C#2 at 2 dai.

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Proteomic characterization of LDIP mutant phenotypes in Arabidopsis seedlings

Project description:Lipid droplets (LDs) are unique, protein-coated organelles found in all eukaryotic organisms that function primarily in the storage of energy-rich neutral lipids, such as triacylglycerols (TAGs). In plants, LDs are found in high abundance in oilseeds, and proteins involved in their formation and activity, such as oleosins, have been well-characterized. Our understanding of LD biogenesis and activity in other cell types, as well as the proteins that regulate these processes, is not as comprehensive. We recently identified and characterized a novel Arabidopsis LD coat protein termed LDIP (LDAP-interacting protein) that regulates LD size and neutral lipid homeostasis in leaf and seed embryonic cells. Here, we show that LDIP plays a distinct role in regulating LD size during biogenesis in leaf cells via interactions with key biogenetic proteins. Localization experiments performed in both plant and insect cells revealed LDIP is necessarily recruited to the LD surface by LDAP3 and binds nascent LDs during early-stage LD formation. Pull-down and Y2H assays indicate LDIP interacts with the biogenetic proteins SEIPINs, while combinatory expression levels of these proteins resulted in aberrant LD size and number in both plant cells and yeast. Evidence is also provided that LDIP plays a key role in modulating phospholipid levels in both leaves and seeds. Taken together, our data allow for the generation of model for LD biogenesis in non-seed cell types.

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Arabidopsis LDIP is an LDAP-interacting protein that influences lipid droplet biogenesis and neutral lipid homeostasis in both leaves and seeds

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Identification of a lipid droplet-plasma membrane tethering complex

Project description:Membrane contact sites (MCS) are interorganellar contacts that allow for the direct exchange of molecules such as lipids or Ca2+ between organelles, but can also be a mean for tethering of organelles. In mammals and yeast, LDs have been shown to engage in MCS with nearly all organelles in the cell, while in plants only LD-ER and LD-peroxisome contacts have been characterised. We here analyse three proteins, LD-localised SEED LIPID DROPLET PROTEIN (SLDP) 1 and 2 and PM-localised LIPID DROPLET PLASMA MEMBRANE ADAPTOR. Knockout of SLDP1 and 2, as well as knockout of LIPA lead to aberrant clustering of LDs in seedlings, while ectopic co-expression of SLDP and LIPA in Nicotiana tabacum pollen tubes is sufficient to reconstitute LD-PM tethering in this tissue, where LDs normally dynamically float in the cytosol stream. We propose a model, in which SLDP and LIPA interact and thereby form a tether to anchor a subset of LDs to the PM during post-germinative growth in Arabidopsis thaliana.

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Arabidopsis EARLY RESPONSIVE TO DEHYDRATION 7 associates with lipid droplets via its senescence domain

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