Proteomics

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Seedling proteome of Arabidopsis thaliana pux10-1 mutants

ABSTRACT: 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.

INSTRUMENT(S): LTQ Orbitrap Velos

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

TISSUE(S): Seedling, Seed

SUBMITTER: Till Ischebeck  

LAB HEAD: Dr. Till Ischebeck

PROVIDER: PXD009207 | Pride | 2018-08-13

REPOSITORIES: Pride

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0daipeptides.txt Txt
0daiproteinGroups.txt Txt
1daipeptides.txt Txt
1daiproteinGroups.txt Txt
2daipeptides.txt Txt
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Publications

PUX10 Is a Lipid Droplet-Localized Scaffold Protein That Interacts with CELL DIVISION CYCLE48 and Is Involved in the Degradation of Lipid Droplet Proteins.

Kretzschmar Franziska K FK   Mengel Laura A LA   Müller Anna O AO   Schmitt Kerstin K   Blersch Katharina F KF   Valerius Oliver O   Braus Gerhard H GH   Ischebeck Till T  

The Plant cell 20180807 9

The number of known proteins associated with plant lipid droplets (LDs) is small compared with other organelles. Many aspects of LD biosynthesis and degradation are unknown, and identifying and characterizing candidate LD proteins could help elucidate these processes. Here, we analyzed the proteome of LD-enriched fractions isolated from tobacco (<i>Nicotiana tabacum</i>) pollen tubes. Proteins that were highly enriched in comparison with the total or cytosolic fraction were further tested for LD  ...[more]

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