Downregulation of a chloroplast-targeted β-amylase leads to a starch-excess phenotype in leaves

被引:187
作者
Scheidig, A [1 ]
Fröhlich, A [1 ]
Schulze, S [1 ]
Lloyd, JR [1 ]
Kossmann, J [1 ]
机构
[1] Max Planck Inst Mol Plant Physiol, Willmitzer Dept, D-14476 Golm, Germany
关键词
beta-amylase; starch degradation; transitory starch; plastid localization; leaf; potato;
D O I
10.1046/j.1365-313X.2002.01317.x
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
A functional screen in Escherichia coli was established to identify potato genes coding for proteins involved in transitory starch degradation. One clone isolated had a sequence very similar to a recently described chloroplast-targeted 5-amylase of Arabidopsis. Expression of the gene in E. coli showed that the protein product was a functional beta-amylase that could degrade both starch granules and solubilized amylopectin, while import experiments demonstrated that the beta-amylase was imported and processed into pea chloroplasts. To study the function of the protein in transitory starch degradation, transgenic potato plants were generated where its activity was reduced using antisense techniques. Analysis of plants reduced in the presence of this beta-amylase isoform showed that their leaves had a starch-excess phenotype, indicating a defect in starch degradation. In addition, it was shown that the antisense plants degraded only 8-30% of their total starch, in comparison with 50% in the wild type, over the dark period. This is the first time that a physiological role for a beta-amylase in plants has been demonstrated.
引用
收藏
页码:581 / 591
页数:11
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