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Proteome of Arabidopsis thaliana pux10-1 mutant lipid droplets

ABSTRACT: 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.

INSTRUMENT(S): LTQ Orbitrap Velos

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

TISSUE(S): Seedling

SUBMITTER: Till Ischebeck

LAB HEAD: Dr. Till Ischebeck

PROVIDER: PXD009248 | Pride | 2018-08-13

REPOSITORIES: Pride

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			Action	DRS
	FK_V_104.raw	Raw
	FK_V_105.raw	Raw
	FK_V_106.raw	Raw
	FK_V_107.raw	Raw
	FK_V_108.raw	Raw

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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.

2018-08-13 | PXD009207 | Pride

Proteome of Arabidopsis thaliana pux10-1 mutant lipid droplets at 1 and 2 days after imbibition

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.

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Seedling proteome of Arabidopsis thaliana pux10-3 mutant

Project description: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.

2018-08-13 | PXD009397 | Pride

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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Nicotiana tabacum seed lipid droplet proteome

Project description:The number of known proteins associated with plant lipid droplets (LDs) is small compared to other organelles. Many questions of LD biosynthesis and degradation remain open, also due to lack of candidate LD proteins whose characterization could help to elucidate their function in those processes. We performed a proteomic screen on LDs isolated from Nicotiana tabacum pollen tubes. Proteins that were highly enriched in the LD fraction compared to the total or cytosolic fraction where verified for LD localization via transient expression in tobacco pollen tubes. We also compared the isoforms of typical LD proteins found in the pollen tubes on a qualitative level to the isoforms found in tobacco seeds.

2018-08-13 | PXD009186 | Pride

Nicotiana tabacum pollen tube lipid droplet proteome

2018-08-13 | PXD009184 | Pride

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

Project description:Cytoplasmic lipid droplets (LDs) are found in all types of plant cells where they are derived from the endoplasmic reticulum (ER) and function as a repository for neutral lipids, as well as serving in lipid remodelling and signalling. However, the mechanisms underlying the formation and functioning of plant LDs, particularly in non-seed tissues, are relatively unknown. Previously, we showed that the LD-Associated Proteins (LDAPs) are a family of plant-specific, LD surface-associated coat proteins that are required for proper LD biogenesis and neutral lipid homeostasis in vegetative tissues. Here, we screened a yeast two-hybrid library using Arabidopsis LDAP3 as ‘bait’ in an effort to identify other novel LD protein constituents. One of the candidate LDAP3-interacting proteins was Arabidopsis At5g16550, which is a plant-specific protein of unknown function that we termed LDIP (LDAP-interacting protein). Using a combination of biochemical and cellular approaches, we show that LDIP targets specifically to the LD surface, contains a discrete amphipathic -helical targeting sequence, and participates in both homotypic and heterotypic associations with itself and LDAP3, respectively. Analysis of LDIP T-DNA knockdown and knockout mutants showed a decrease in LD abundance and increase in variability of LD size in leaves, with concomitant increases in total neutral lipid content. Similar phenotypes were observed in plant seeds, which showed enlarged LDs and increases in total seed oil amounts. Collectively, these data identify LDIP as a new player in LD biogenesis in plants that modulates both LD size and cellular neutral lipid homeostasis. Potential mechanisms of LDIP activity are discussed.

2017-11-06 | PXD007192 | Pride

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.

2022-02-15 | PXD012992 | Pride

OsNOA1 functions in a threshold-dependent manner to regulate chloroplast proteins in rice at lower temperatures

Project description:While our earlier microarray analysis identified a number of possible candidate genes, which may be involved in OsNOA1 function (Yang et al., 2011a), a complementary study of the rice proteome profiles under the same condition has the potential to yield new insights into the biological functions of NOA1 and molecular mechanism of NOA1 associated regulation. In this study, we utilized previously-generated OsNOA1 RNAi lines (Yang et al., 2011a) and newly-generated OsNOA1 overexpression lines to further investigate the function and mechanism of NOA1 in rice. Here we report the proteome changes which include important candidate proteins involved in chloroplast ribosome biogenesis and several classes of proteins with significant changes in response to various levels of OsNOA1 under two different temperature conditions. Our results suggest that OsNOA1 can function in a threshold-dependent manner to regulate the biosynthesis of chloroplast proteins in rice at lower temperatures, and this regulation may be achieved via interactions between NOA1 and chloroplast ribosomes.

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