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  The Interconversion of UDP-Arabinopyranose and UDP-Arabinofuranose Is Indispensable for Plant Development in Arabidopsis

Rautengarten, C., Ebert, B., Herter, T., Petzold, C. J., Ishii, T., Mukhopadhyay, A., et al. (2011). The Interconversion of UDP-Arabinopyranose and UDP-Arabinofuranose Is Indispensable for Plant Development in Arabidopsis. Plant Cell, 23(4), 1373-1390. doi:10.1105/tpc.111.083931.

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Rautengarten-2011-The Interconversion.pdf (beliebiger Volltext), 2MB
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Rautengarten-2011-The Interconversion.pdf
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Rautengarten, C.1, Autor
Ebert, B.2, Autor           
Herter, T.3, Autor           
Petzold, C. J.1, Autor
Ishii, T.1, Autor
Mukhopadhyay, A.1, Autor
Usadel, B.3, Autor           
Scheller, H. V.1, Autor
Affiliations:
1External Organizations, ou_persistent22              
2Biophysical Analysis, Infrastructure Groups and Service Units, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753307              
3Integrative Carbon Biology, Department Stitt, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753329              

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Schlagwörter: reversibly glycosylated polypeptide seed coat development rhamnogalacturonan-i arabinosyltransferase activity biochemical-characterization protein transglucosylase molecular-cloning complex-formation pectic arabinan biosynthesis
 Zusammenfassung: L-Ara, an important constituent of plant cell walls, is found predominantly in the furanose rather than in the thermodynamically more stable pyranose form. Nucleotide sugar mutases have been demonstrated to interconvert UDP-L-arabinopyranose (UDP-Arap) and UDP-L-arabinofuranose (UDP-Araf) in rice (Oryza sativa). These enzymes belong to a small gene family encoding the previously named Reversibly Glycosylated Proteins (RGPs). RGPs are plant-specific cytosolic proteins that tend to associate with the endomembrane system. In Arabidopsis thaliana, the RGP protein family consists of five closely related members. We characterized all five RGPs regarding their expression pattern and subcellular localizations in transgenic Arabidopsis plants. Enzymatic activity assays of recombinant proteins expressed in Escherichia coli identified three of the Arabidopsis RGP protein family members as UDP-L-Ara mutases that catalyze the formation of UDP-Araf from UDP-Arap. Coimmunoprecipitation and subsequent liquid chromatography-electrospray ionization-tandem mass spectrometry analysis revealed a distinct interaction network between RGPs in different Arabidopsis organs. Examination of cell wall polysaccharide preparations from RGP1 and RGP2 knockout mutants showed a significant reduction in total L-Ara content (12-31%) compared with wild-type plants. Concomitant downregulation of RGP1 and RGP2 expression results in plants almost completely deficient in cell wall-derived L-Ara and exhibiting severe developmental defects.

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Sprache(n): eng - English
 Datum: 2011-04-082011
 Publikationsstatus: Erschienen
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 Identifikatoren: ISI: ISI:000291000500018
DOI: 10.1105/tpc.111.083931
ISSN: 1040-4651
URI: ://000291000500018 http://www.plantcell.org/content/23/4/1373.full.pdf
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Titel: Plant Cell
Genre der Quelle: Zeitschrift
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Seiten: - Band / Heft: 23 (4) Artikelnummer: - Start- / Endseite: 1373 - 1390 Identifikator: -