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Glucan, water dikinase activity stimulates breakdown of starch granules by plastidial β-amylases

Glucan phosphorylating enzymes are required for normal mobilization of starch in leaves of Arabidopsis (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 fr...

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Main Authors: Christoph, Edner, Jing, Li, Tanja, Albrecht, Sebastian, Mahlow, Mahdi, Hejazi, Hasnain, Hussain, Fatma, Kaplan, Charles, Guy, Steven M., Smith, Martin, Steup, Gerhard, Ritte
Format: E-Article
Language:English
Published: American Society of Plant Biologists 2007
Subjects:
Q Science (General)
SB Plant culture
Online Access:http://ir.unimas.my/id/eprint/9975/1/Glucan%2C%20Water%20Dikinase%20Activity%20Stimulates%20Breakdown%20of%20Starch%20Granules%20by%20Plastidial%20%CE%B2-Amylases%20%28abstract%29.pdf
http://ir.unimas.my/id/eprint/9975/
https://scholar.google.com/citations?view_op=view_citation&hl=uk&user=F_urR10AAAAJ&citation_for_view=F_urR10AAAAJ:W7OEmFMy1HYC
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spelling my.unimas.ir.99752015-12-08T03:36:08Z http://ir.unimas.my/id/eprint/9975/ Glucan, water dikinase activity stimulates breakdown of starch granules by plastidial β-amylases Christoph, Edner Jing, Li Tanja, Albrecht Sebastian, Mahlow Mahdi, Hejazi Hasnain, Hussain Fatma, Kaplan Charles, Guy Steven M., Smith Martin, Steup Gerhard, Ritte Q Science (General) SB Plant culture Glucan phosphorylating enzymes are required for normal mobilization of starch in leaves of Arabidopsis (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 2-fold if the granules were simultaneously phosphorylated by recombinant potato glucan, water dikinase (GWD). Using matrix-assisted laser-desorption ionization mass spectrometry several putative starch-related enzymes were identified in this fraction, among them b-AMYLASE1 (BAM1; At3g23920) and ISOAMYLASE3 (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 2 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 b-amylase isoform, increased 2- to 3-fold 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. American Society of Plant Biologists 2007 E-Article NonPeerReviewed text en http://ir.unimas.my/id/eprint/9975/1/Glucan%2C%20Water%20Dikinase%20Activity%20Stimulates%20Breakdown%20of%20Starch%20Granules%20by%20Plastidial%20%CE%B2-Amylases%20%28abstract%29.pdf Christoph, Edner and Jing, Li and Tanja, Albrecht and Sebastian, Mahlow and Mahdi, Hejazi and Hasnain, Hussain and Fatma, Kaplan and Charles, Guy and Steven M., Smith and Martin, Steup and Gerhard, Ritte (2007) Glucan, water dikinase activity stimulates breakdown of starch granules by plastidial β-amylases. Plant Physiology, 145 (1). pp. 17-28. ISSN 1532-2548 https://scholar.google.com/citations?view_op=view_citation&hl=uk&user=F_urR10AAAAJ&citation_for_view=F_urR10AAAAJ:W7OEmFMy1HYC doi : 10.1104/pp.107.104224
institution Universiti Malaysia Sarawak
building Centre for Academic Information Services (CAIS)
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Malaysia Sarawak
content_source UNIMAS Institutional Repository
url_provider http://ir.unimas.my/
language English
topic Q Science (General)
SB Plant culture
spellingShingle Q Science (General)
SB Plant culture
Christoph, Edner
Jing, Li
Tanja, Albrecht
Sebastian, Mahlow
Mahdi, Hejazi
Hasnain, Hussain
Fatma, Kaplan
Charles, Guy
Steven M., Smith
Martin, Steup
Gerhard, Ritte
Glucan, water dikinase activity stimulates breakdown of starch granules by plastidial β-amylases
description Glucan phosphorylating enzymes are required for normal mobilization of starch in leaves of Arabidopsis (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 2-fold if the granules were simultaneously phosphorylated by recombinant potato glucan, water dikinase (GWD). Using matrix-assisted laser-desorption ionization mass spectrometry several putative starch-related enzymes were identified in this fraction, among them b-AMYLASE1 (BAM1; At3g23920) and ISOAMYLASE3 (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 2 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 b-amylase isoform, increased 2- to 3-fold 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.
format E-Article
author Christoph, Edner
Jing, Li
Tanja, Albrecht
Sebastian, Mahlow
Mahdi, Hejazi
Hasnain, Hussain
Fatma, Kaplan
Charles, Guy
Steven M., Smith
Martin, Steup
Gerhard, Ritte
author_facet Christoph, Edner
Jing, Li
Tanja, Albrecht
Sebastian, Mahlow
Mahdi, Hejazi
Hasnain, Hussain
Fatma, Kaplan
Charles, Guy
Steven M., Smith
Martin, Steup
Gerhard, Ritte
author_sort Christoph, Edner
title Glucan, water dikinase activity stimulates breakdown of starch granules by plastidial β-amylases
title_short Glucan, water dikinase activity stimulates breakdown of starch granules by plastidial β-amylases
title_full Glucan, water dikinase activity stimulates breakdown of starch granules by plastidial β-amylases
title_fullStr Glucan, water dikinase activity stimulates breakdown of starch granules by plastidial β-amylases
title_full_unstemmed Glucan, water dikinase activity stimulates breakdown of starch granules by plastidial β-amylases
title_sort glucan, water dikinase activity stimulates breakdown of starch granules by plastidial β-amylases
publisher American Society of Plant Biologists
publishDate 2007
url http://ir.unimas.my/id/eprint/9975/1/Glucan%2C%20Water%20Dikinase%20Activity%20Stimulates%20Breakdown%20of%20Starch%20Granules%20by%20Plastidial%20%CE%B2-Amylases%20%28abstract%29.pdf
http://ir.unimas.my/id/eprint/9975/
https://scholar.google.com/citations?view_op=view_citation&hl=uk&user=F_urR10AAAAJ&citation_for_view=F_urR10AAAAJ:W7OEmFMy1HYC
_version_ 1644510859599282176
score 13.211869

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