A proteomic analysis of organelles fromArabidopsis thaliana

Prime, Tracy A.; Sherrier, D. Janine; Mahon, Piers; Packman, Len C.; Dupree, Paul

doi:10.1002/1522-2683(20001001)21:16<3488::aid-elps3488>3.0.co;2-3

Cited by 122 publications

(90 citation statements)

References 58 publications

(50 reference statements)

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“…V-type ATPases are known constituents of animal DRMs (21,40) and, even though they are primarily vacuolar in plants, there is evidence that they are also present in the plasma membranes of plant cells (58,60). In addition, several recent reports have shown an enrichment of V-type ATPases in DRMs from Arabidopsis thaliana (6), Nicotiana tabacum (51), and Medicago truncatula (39).…”

Section: Discussionmentioning

confidence: 99%

Cell Wall Polysaccharide Synthases Are Located in Detergent-Resistant Membrane Microdomains in Oomycetes

Briolay

Bouzenzana

Guichardant

et al. 2009

Appl Environ Microbiol

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Section: Discussionmentioning

confidence: 99%

Cell Wall Polysaccharide Synthases Are Located in Detergent-Resistant Membrane Microdomains in Oomycetes

Briolay

Bouzenzana

Guichardant

et al. 2009

Appl Environ Microbiol

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“…Callus grown in liquid culture was generated and maintained as described previously (Prime et al, 2000). NDP-sugars were extracted according to a previously described method (Lunn et al, 2006) with slight modifications.…”

Section: Ndp-sugar Analysis By Lc-ms/msmentioning

confidence: 99%

KONJAC1 and 2 Are Key Factors for GDP-Mannose Generation and Affect l-Ascorbic Acid and Glucomannan Biosynthesis in Arabidopsis

et al. 2015

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Humans are unable to synthesize L-ascorbic acid (AsA), yet it is required as a cofactor in many critical biochemical reactions. The majority of human dietary AsA is obtained from plants. In Arabidopsis thaliana, a GDP-mannose pyrophosphorylase (GMPP), VITAMIN C DEFECTIVE1 (VTC1), catalyzes a rate-limiting step in AsA synthesis: the formation of GDP-Man. In this study, we identified two nucleotide sugar pyrophosphorylase-like proteins, KONJAC1 (KJC1) and KJC2, which stimulate the activity of VTC1. The kjc1kjc2 double mutant exhibited severe dwarfism, indicating that KJC proteins are important for growth and development. The kjc1 mutation reduced GMPP activity to 10% of wild-type levels, leading to a 60% reduction in AsA levels. On the contrary, overexpression of KJC1 significantly increased GMPP activity. The kjc1 and kjc1kjc2 mutants also exhibited significantly reduced levels of glucomannan, which is also synthesized from GDP-Man. Recombinant KJC1 and KJC2 enhanced the GMPP activity of recombinant VTC1 in vitro, while KJCs did not show GMPP activity. Yeast two-hybrid assays suggested that the stimulation of GMPP activity occurs via interaction of KJCs with VTC1. These results suggest that KJCs are key factors for the generation of GDP-Man and affect AsA level and glucomannan accumulation through the stimulation of VTC1 GMPP activity.

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“…The transgenic line 35S::GTL6-myc was used, expressing a Golgi apparatus marker protein (Gtl6/At2g29900) fused with a c-Myc tag. The conditions of growth were as described in Prime et al, 2000.…”

Section: Plant Materials and Growth Conditionsmentioning

confidence: 99%

Label-Free Protein Quantification for Plant Golgi Protein Localization and Abundance

et al. 2014

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The proteomic composition of the Arabidopsis (Arabidopsis thaliana) Golgi apparatus is currently reasonably well documented; however, little is known about the relative abundances between different proteins within this compartment. Accurate quantitative information of Golgi resident proteins is of great importance: it facilitates a better understanding of the biochemical processes that take place within this organelle, especially those of different polysaccharide synthesis pathways. Golgi resident proteins are challenging to quantify because the abundance of this organelle is relatively low within the cell. In this study, an organelle fractionation approach targeting the Golgi apparatus was combined with a label-free quantitative mass spectrometry (dataindependent acquisition method using ion mobility separation known as LC-IMS-MS E [or HDMS E ]) to simultaneously localize proteins to the Golgi apparatus and assess their relative quantity. In total, 102 Golgi-localized proteins were quantified. These data show that organelle fractionation in conjunction with label-free quantitative mass spectrometry is a powerful and relatively simple tool to access protein organelle localization and their relative abundances. The findings presented open a unique view on the organization of the plant Golgi apparatus, leading toward unique hypotheses centered on the biochemical processes of this organelle.

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A proteomic analysis of organelles fromArabidopsis thaliana

Cited by 122 publications

References 58 publications

Cell Wall Polysaccharide Synthases Are Located in Detergent-Resistant Membrane Microdomains in Oomycetes

Cell Wall Polysaccharide Synthases Are Located in Detergent-Resistant Membrane Microdomains in Oomycetes

KONJAC1 and 2 Are Key Factors for GDP-Mannose Generation and Affect l-Ascorbic Acid and Glucomannan Biosynthesis in Arabidopsis

Label-Free Protein Quantification for Plant Golgi Protein Localization and Abundance

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