Plant Physiol. Illumina
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

First published online April 22, 2005; 10.1104/pp.105.059295

Plant Physiology 138:184-195 (2005)
© 2005 American Society of Plant Biologists

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental Data
Right arrow All Versions of this Article:
138/1/184    most recent
pp.105.059295v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Wattebled, F.
Right arrow Articles by D'Hulst, C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Wattebled, F.
Right arrow Articles by D'Hulst, C.
Agricola
Right arrow Articles by Wattebled, F.
Right arrow Articles by D'Hulst, C.
BIOCHEMICAL PROCESSES AND MACROMOLECULAR STRUCTURES

Mutants of Arabidopsis Lacking a Chloroplastic Isoamylase Accumulate Phytoglycogen and an Abnormal Form of Amylopectin1,[w]

Fabrice Wattebled2, Ying Dong2, Sylvain Dumez, David Delvallé, Véronique Planchot, Pierre Berbezy, Darshna Vyas, Paul Colonna, Manash Chatterjee3, Steven Ball and Christophe D'Hulst*

Unité de Glycobiologie Structurale et Fonctionnelle, Unité Mixte de Recherche 8576 Centre National de la Recherche Scientifique, Université des Sciences et Technologies de Lille, 59655 Villeneuve d'Ascq cedex, France (F.W., Y.D., S.D., D.D., S.B., C.D.); Unité de Recherche sur les Biopolymères, Intéractions et Assemblages, Institut National de la Recherche Agronomique Centre de Nantes, 44316 Nantes cedex 3, France (V.P., P.C.); and Biogemma UK Ltd, Cambridge CB4 0GZ, United Kingdom (P.B., D.V., M.C.)

Mutant lines defective for each of the four starch debranching enzyme (DBE) genes (AtISA1, AtISA2, AtISA3, and AtPU1) detected in the nuclear genome of Arabidopsis (Arabidopsis thaliana) were produced and analyzed. Our results indicate that both AtISA1 and AtISA2 are required for the production of a functional isoamylase-type of DBE named Iso1, the major isoamylase activity found in leaves. The absence of Iso1 leads to an 80% decrease in the starch content in both lines and to the accumulation of water-soluble polysaccharides whose structure is similar to glycogen. In addition, the residual amylopectin structure in the corresponding mutant lines displays a strong modification when compared to the wild type, suggesting a direct, rather than an indirect, function of Iso1 during the synthesis of amylopectin. Mutant lines carrying a defect in AtISA3 display a strong starch-excess phenotype at the end of both the light and the dark phases accompanied by a small modification of the amylopectin structure. This result suggests that this isoamylase-type of DBE plays a major role during starch mobilization. The analysis of the Atpu1 single-mutant lines did not lead to a distinctive phenotype. However, Atisa2/Atpu1 double-mutant lines display a 92% decrease in starch content. This suggests that the function of pullulanase partly overlaps that of Iso1, although its implication remains negligible when Iso1 is present within the cell.

1 This work was supported by Génoplante (project no. Af2001030), by the Région Nord Pas de Calais, by the Ministère Délégué à la Recherche (Action Concertée Incitative Jeunes-Chercheurs no. JC5145), by the European Community (Feder, CPER2000–2006), and by the Centre National de la Recherche Scientifique.

2 These authors contributed equally to the paper.

3 Present address: National Institute of Agricultural Biology, Hintingdon Road, Cambridge CB3 0LE, UK.

[w] The online version of this article contains Web-only data.

Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.105.059295.

* Corresponding author; e-mail christophe.dhulst{at}univ-lille1.fr; fax 33–3–20–43–65–55.

Received January 26, 2005; returned for revision March 1, 2005; accepted March 3, 2005.




This article has been cited by other articles:


Home page
 Plant Physiol.Home page
S. Comparot-Moss, O. Kotting, M. Stettler, C. Edner, A. Graf, S. E. Weise, S. Streb, W.-L. Lue, D. MacLean, S. Mahlow, et al.
A Putative Phosphatase, LSF1, Is Required for Normal Starch Turnover in Arabidopsis Leaves
Plant Physiology, February 1, 2010; 152(2): 685 - 697.
[Abstract] [Full Text] [PDF]

Home page
 J Exp BotHome page
F. Liu, A. Makhmoudova, E. A. Lee, R. Wait, M. J. Emes, and I. J. Tetlow
The amylose extender mutant of maize conditions novel protein-protein interactions between starch biosynthetic enzymes in amyloplasts
J. Exp. Bot., November 1, 2009; 60(15): 4423 - 4440.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
N. Szydlowski, P. Ragel, S. Raynaud, M. M. Lucas, I. Roldan, M. Montero, F. J. Munoz, M. Ovecka, A. Bahaji, V. Planchot, et al.
Starch Granule Initiation in Arabidopsis Requires the Presence of Either Class IV or Class III Starch Synthases
PLANT CELL, August 1, 2009; 21(8): 2443 - 2457.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
V. V. Radchuk, L. Borisjuk, N. Sreenivasulu, K. Merx, H.-P. Mock, H. Rolletschek, U. Wobus, and W. Weschke
Spatiotemporal Profiling of Starch Biosynthesis and Degradation in the Developing Barley Grain
Plant Physiology, May 1, 2009; 150(1): 190 - 204.
[Abstract] [Full Text] [PDF]

Home page
 J Exp BotHome page
N. Fujita, Y. Toyosawa, Y. Utsumi, T. Higuchi, I. Hanashiro, A. Ikegami, S. Akuzawa, M. Yoshida, A. Mori, K. Inomata, et al.
Characterization of pullulanase (PUL)-deficient mutants of rice (Oryza sativa L.) and the function of PUL on starch biosynthesis in the developing rice endosperm
J. Exp. Bot., March 1, 2009; 60(3): 1009 - 1023.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
S. Streb, T. Delatte, M. Umhang, S. Eicke, M. Schorderet, D. Reinhardt, and S. C. Zeeman
Starch Granule Biosynthesis in Arabidopsis Is Abolished by Removal of All Debranching Enzymes but Restored by the Subsequent Removal of an Endoamylase
PLANT CELL, December 1, 2008; 20(12): 3448 - 3466.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
F. Wattebled, V. Planchot, Y. Dong, N. Szydlowski, B. Pontoire, A. Devin, S. Ball, and C. D'Hulst
Further Evidence for the Mandatory Nature of Polysaccharide Debranching for the Aggregation of Semicrystalline Starch and for Overlapping Functions of Debranching Enzymes in Arabidopsis Leaves
Plant Physiology, November 1, 2008; 148(3): 1309 - 1323.
[Abstract] [Full Text] [PDF]

Home page
 J Exp BotHome page
J. C. Cushman, R. L. Tillett, J. A. Wood, J. M. Branco, and K. A. Schlauch
Large-scale mRNA expression profiling in the common ice plant, Mesembryanthemum crystallinum, performing C3 photosynthesis and Crassulacean acid metabolism (CAM)
J. Exp. Bot., May 1, 2008; 59(7): 1875 - 1894.
[Abstract] [Full Text] [PDF]

Home page
 GeneticsHome page
P. Deschamps, H. Moreau, A. Z. Worden, D. Dauvillee, and S. G. Ball
Early Gene Duplication Within Chloroplastida and Its Correspondence With Relocation of Starch Metabolism to Chloroplasts
Genetics, April 1, 2008; 178(4): 2373 - 2387.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
D. C. Fulton, M. Stettler, T. Mettler, C. K. Vaughan, J. Li, P. Francisco, M. Gil, H. Reinhold, S. Eicke, G. Messerli, et al.
{beta}-AMYLASE4, a Noncatalytic Protein Required for Starch Breakdown, Acts Upstream of Three Active {beta}-Amylases in Arabidopsis Chloroplasts
PLANT CELL, April 1, 2008; 20(4): 1040 - 1058.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
I. J. Tetlow, K. G. Beisel, S. Cameron, A. Makhmoudova, F. Liu, N. S. Bresolin, R. Wait, M. K. Morell, and M. J. Emes
Analysis of Protein Complexes in Wheat Amyloplasts Reveals Functional Interactions among Starch Biosynthetic Enzymes
Plant Physiology, April 1, 2008; 146(4): 1878 - 1891.
[Abstract] [Full Text] [PDF]

Home page
 Mol Biol EvolHome page
P. Deschamps, C. Colleoni, Y. Nakamura, E. Suzuki, J.-L. Putaux, A. Buleon, S. Haebel, G. Ritte, M. Steup, L. I. Falcon, et al.
Metabolic Symbiosis and the Birth of the Plant Kingdom
Mol. Biol. Evol., March 1, 2008; 25(3): 536 - 548.
[Abstract] [Full Text] [PDF]

Home page
 Eukaryot CellHome page
C. Plancke, C. Colleoni, P. Deschamps, D. Dauvillee, Y. Nakamura, S. Haebel, G. Ritte, M. Steup, A. Buleon, J.-L. Putaux, et al.
Pathway of Cytosolic Starch Synthesis in the Model Glaucophyte Cyanophora paradoxa
Eukaryot. Cell, February 1, 2008; 7(2): 247 - 257.
[Abstract] [Full Text] [PDF]

Home page
 J Exp BotHome page
L. Li, H. Ilarslan, M. G. James, A. M. Myers, and E. S. Wurtele
Genome wide co-expression among the starch debranching enzyme genes AtISA1, AtISA2, and AtISA3 in Arabidopsis thaliana
J. Exp. Bot., September 20, 2007; (2007) erm180v1.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
C. Edner, J. Li, T. Albrecht, S. Mahlow, M. Hejazi, H. Hussain, F. Kaplan, C. Guy, S. M. Smith, M. Steup, et al.
Glucan, Water Dikinase Activity Stimulates Breakdown of Starch Granules by Plastidial beta-Amylases
Plant Physiology, September 1, 2007; 145(1): 17 - 28.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
G. Messerli, V. Partovi Nia, M. Trevisan, A. Kolbe, N. Schauer, P. Geigenberger, J. Chen, A. C. Davison, A. R. Fernie, and S. C. Zeeman
Rapid Classification of Phenotypic Mutants of Arabidopsis via Metabolite Fingerprinting
Plant Physiology, April 1, 2007; 143(4): 1484 - 1492.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
S. Dumez, F. Wattebled, D. Dauvillee, D. Delvalle, V. Planchot, S. G. Ball, and C. D'Hulst
Mutants of Arabidopsis Lacking Starch Branching Enzyme II Substitute Plastidial Starch Synthesis by Cytoplasmic Maltose Accumulation
PLANT CELL, October 1, 2006; 18(10): 2694 - 2709.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
T. Delatte, M. Umhang, M. Trevisan, S. Eicke, D. Thorneycroft, S. M. Smith, and S. C. Zeeman
Evidence for Distinct Mechanisms of Starch Granule Breakdown in Plants
J. Biol. Chem., April 28, 2006; 281(17): 12050 - 12059.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
T. Niittyla, S. Comparot-Moss, W.-L. Lue, G. Messerli, M. Trevisan, M. D. J. Seymour, J. A. Gatehouse, D. Villadsen, S. M. Smith, J. Chen, et al.
Similar Protein Phosphatases Control Starch Metabolism in Plants and Glycogen Metabolism in Mammals
J. Biol. Chem., April 28, 2006; 281(17): 11815 - 11818.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 2005 by the American Society of Plant Biologists