Plant Physiology Preview
Published on July 13, 2007; 10.1104/pp.107.104224
OPEN ACCESS ARTICLE
Received June 18, 2007
Accepted July 11, 2007
Glucan, Water Dikinase Activity Stimulates Breakdown of Starch Granules by Plastidial beta-amylases
Christoph Edner , Jing Li , Tanja Albrecht , Sebastian Mahlow , Mahdi Hejazi , Hasnain Hussain , Fatma Kaplan , Charles Guy , Steven M. Smith , Martin Steup , and Gerhard Ritte *
Plant Physiology, Institute of Biochemistry and Biology, University of Potsdam, Karl-Liebknecht-Str. 24-25, Building 20, 14476 Potsdam-Golm, Germany; ARC Centre of Excellence in Plant Energy Biology, University of Western Australia, Crawley, WA 6009, Australia; Molecular Biology, University Malaysia Sarawak, 94300 Kota Samarahan, Sarawak, Malaysia; Department of Environmental Horticulture, University of Florida, Gainesville, Florida 32611, USA
* Corresponding author; email: ritte{at}uni-potsdam.de.
Glucan phosphorylating enzymes are required for normal mobilization of starch in leaves of Arabidopsis thaliana and potato (Solanum tuberosum), but mechanisms underlying this dependency are unknown. Using two different activity assays, we aimed to identify starch degrading enzymes from Arabidopsis, whose activity is affected by glucan phosphorylation. Breakdown of granular starch by a protein fraction purified from leaf extracts increased approximately twofold if the granules were simultaneously phosphorylated by recombinant potato GWD. Using MALDI-MS several putative starch-related enzymes were identified in this fraction among them  -amylase 1 (BAM1, At3g23920) and isoamylase 3 (ISA3, At4g09020). Experiments using purified recombinant enzymes showed that BAM1 activity with granules similarly increased under conditions of simultaneous starch phosphorylation. Purified recombinant potato ISA3 (StISA3) did not attack the granular starch significantly with or without glucan phosphorylation. However, starch breakdown by a mixture of BAM1 and StISA3 was two times higher than that by BAM1 alone and was further enhanced in the presence of GWD and ATP. Similar to BAM1, maltose release from granular starch by purified recombinant BAM3 (At4g17090), another plastid-localized -amylase isoform, increased two- to threefold if the granules were simultaneously phosphorylated by GWD. BAM activity in turn strongly stimulated the GWD-catalyzed phosphorylation. The interdependence between the activities of GWD and BAMs offers an explanation for the severe starch excess phenotype of GWD-deficient mutants.
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