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          Institute: MPI für molekulare Pflanzenphysiologie     Collection: Publikationen Pflanzenphysiologie     Display Documents

ID: 251391.0, MPI für molekulare Pflanzenphysiologie / Publikationen Pflanzenphysiologie
Identification, subcellular localization and biochemical characterization of water-soluble heteroglycans (SHG) in leaves of Arabidopsis thaliana L.: distinct SHG reside in the cytosol and in the apoplast
Authors:Fettke, J.; Eckermann, N.; Tiessen, A.; Geigenberger, P.; Steup, M.
Date of Publication (YYYY-MM-DD):2005-08
Title of Journal:Plant Journal
Journal Abbrev.:Plant J
Issue / Number:4
Start Page:568
End Page:585
Review Status:not specified
Audience:Not Specified
Abstract / Description:Water-soluble heteroglycans (SHG) were isolated from leaves of wild-type Arabidopsis thaliana L. and from two starch-deficient mutants. Major constituents of the SHG are arabinose, galactose, rhamnose, and glucose. SHG was separated into low (< 10 kDa; SHG(S)) and high (> 10 kDa; SHG(L)) molecular weight compounds. SHG(S) was resolved into approximately 25 distinct oligoglycans by ion exchange chromatography. SHG(L) was further separated into two subfractions, designated as subfraction I and II, by field flow fractionation. For the intracellular localization of the various SHG compounds several approaches were chosen: first, leaf material was subjected to non-aqueous fractionation. The apolar gradient fractions were characterized by monitoring markers and were used as starting material for the SHG isolation. Subfraction I and SHG(S) exhibited a distribution similar to that of cytosolic markers whereas subfraction II cofractionated with crystalline cellulose. Secondly, intact organelles were isolated and used for SHG isolation. Preparations of intact organelles (mitochondria plus peroxisomes) contained no significant amount of any heteroglycan. In isolated intact microsomes a series of oligoglycans was recovered but neither subfraction I nor II. In in vitro assays using glucose 1-phosphate and recombinant cytosolic (Pho 2) phosphorylase both SHG(S) and subfraction I acted as glucosyl acceptor whereas subfraction II was essentially inactive. Rabbit muscle phosphorylase a did not utilize any of the plant glycans indicating a specific Pho 2-glycan interaction. As revealed by in vivo labeling experiments using (CO2)-C-14 carbon fluxes into subfraction I and II differed. Furthermore, in leaves the pool size of subfraction I varied during the light-dark regime.
Free Keywords:carbohydrate metabolism
; heteroglycan
; subcellular localization
; non-aqueous fractionation
; carbon fluxes
; arabidopsis thaliana
; adp-glucose pyrophosphorylase
; solanum-tuberosum l.
; pisum-sativum l
; starch degradation
; potato-tubers
; alpha-1,4-glucan phosphorylase
; indirect immunofluorescence
; transitory starch
; spinach leaves
; r1 protein
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für molekulare Pflanzenphysiologie/Metabolische Netzwerke/AG Geigenberger
External Affiliations:Univ Potsdam, Inst Biochem & Biophys, Dept Plant Physiol, Karl Liebknecht Str 24-25,Bldg 20, D-14476 Potsdam, Germany
Univ Potsdam, Inst Biochem & Biophys, Dept Plant Physiol, D-14476 Potsdam, Germany
Max Planck Inst Mol Plant Physiol, D-14476 Potsdam, Germany
Identifiers:ISI:000230889200009 [ID No:1]
ISI:000230889200009 [ID No:2]
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