Proteomics

Dataset Information

0

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

Dataset's files

Source:
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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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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