TY  - JOUR
A1  - Usadel, Björn
A1  - Kuschinsky, Anja M.
A1  - Rosso, Mario G.
A1  - Eckermann, Nora
A1  - Pauly, Markus
T1  - RHM2 is involved in mucilage pectin synthesis and is required for the development of the seed coat in Arabidopsis
N2  - Pectins are major components of primary plant cell walls and the seed mucilage of Arabidopsis. Despite progress in the structural elucidation of pectins, only very few enzymes participating in or regulating their synthesis have been identified. A first candidate gene involved-in the synthesis of pectinaceous rhamnogalacturonan I is RHM2, a putative plant ortholog to NDP-rhamnose biosynthetic enzymes in bacteria. Expression studies with a promoter beta-glucuronidase construct and reverse transcription PCR data show that RHM2 is expressed ubiquitously. Rhm2 T-DNA insertion mutant lines were identified using a reverse genetics approach. Analysis of the rhm2 seeds by various staining methods and chemical analysis of the mucilage revealed a strong reduction of rhamnogalacturonan I in the mucilage and a decrease of its molecular weight. In addition, scanning electron microscopy of the seed surface indicated a distorted testa morphology, illustrating not only a structural but also a developmental role for RGI or rhamnose metabolism in proper testa formation
Y1  - 2004
ER  - 
TY  - JOUR
A1  - Baumann, Guido
A1  - Eckermann, Nora
A1  - Meinel, Thomas
T1  - Zur Kohlenstoffassimilation in grünen Zuckerrüben-Kalluskulturen
Y1  - 1994
ER  - 
TY  - JOUR
A1  - Baumann, Ingrid
A1  - Eckermann, Nora
T1  - Ploidy level and chlorophyll content of single plastids and cells from callus cultures during conversion to autotrophic growth
Y1  - 1994
ER  - 
TY  - THES
A1  - Eckermann, Nora
T1  - Biochemische Charakterisierung von Gewebekulturstämmen unterschiedlicher Photosynthese- und Morphogenesekapazität aus Beta vulgaris L
Y1  - 1995
ER  - 
TY  - JOUR
A1  - Eckermann, Nora
A1  - Baumann, Guido
T1  - Enzymatic changes in callus cultures of sugar beet during the transition from photoheterotrophic to photoautotrophic growth
Y1  - 1995
ER  - 
TY  - JOUR
A1  - Baumann, Ingrid
A1  - Eckermann, Nora
A1  - Krause, Udo
A1  - Baumann, Guido
T1  - Effects of sucrose in the culture medium on cytological characteristics, pigments and photosynthetic activity of green callus cultures of sugar beet
Y1  - 1994
ER  - 
TY  - JOUR
A1  - Fettke, Jörg
A1  - Eckermann, Nora
A1  - Tiessen, Axel
A1  - Geigenberger, Peter Ludwig
A1  - Steup, Martin
T1  - 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
N2  - 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
Y1  - 2005
SN  - 0960-7412
ER  - 
TY  - JOUR
A1  - Ritte, Gerhard
A1  - Lloyd, James R.
A1  - Eckermann, Nora
A1  - Rottmann, Antje
A1  - Kossmann, Jens
A1  - Steup, Martin
T1  - The starch-related R1 protein is an a-glucan, water dikinase
Y1  - 2002
SN  - 0027-8424
ER  - 
TY  - JOUR
A1  - Eckermann, Nora
A1  - Fettke, Jörg
A1  - Steup, Martin
T1  - Identification of polysaccharide binding proteins by affinity electrophoresis in inhomogeneous polyacrylamide gels and subsequent SDS-PAGE/MALDI-TOF analysis
Y1  - 2002
ER  - 
TY  - JOUR
A1  - Ritte, Gerhard
A1  - Eckermann, Nora
A1  - Haebel, Sophie
A1  - Lorberth, Ruth
A1  - Steup, Martin
T1  - Compartmentation of the starch-related R1 protein in higher plants
Y1  - 2000
ER  -