• Media type: E-Article
  • Title: Overexpression of thioredoxin h leads to enhanced activity of starch debranching enzyme (pullulanase) in barley grain
  • Contributor: Cho, Myeong-Je; Wong, Joshua H.; Marx, Corina; Jiang, Wen; Lemaux, Peggy G.; Buchanan, Bob B.
  • imprint: Proceedings of the National Academy of Sciences, 1999
  • Published in: Proceedings of the National Academy of Sciences
  • Language: English
  • DOI: 10.1073/pnas.96.25.14641
  • ISSN: 1091-6490; 0027-8424
  • Origination:
  • Footnote:
  • Description: <jats:p> Biochemically active wheat thioredoxin <jats:italic>h</jats:italic> has been overexpressed in the endosperm of transgenic barley grain. Two DNA constructs containing the wheat thioredoxin <jats:italic>h</jats:italic> gene ( <jats:italic>wtrxh</jats:italic> ) were used for transformation; each contained <jats:italic>wtrxh</jats:italic> fused to an endosperm-specific B <jats:sub>1</jats:sub> -hordein promoter either with or without a signal peptide sequence for targeting to the protein body. Twenty-two stable, independently transformed regenerable lines were obtained by selecting with the herbicide bialaphos to test for the presence of the <jats:italic>bar</jats:italic> herbicide resistance gene on a cotransformed plasmid; all were positive for this gene. The presence of <jats:italic>wtrxh</jats:italic> was confirmed in 20 lines by PCR analysis, and the identity and level of expression of wheat thioredoxin <jats:italic>h</jats:italic> was assessed by immunoblots. Although levels varied among the different transgenic events, wheat thioredoxin <jats:italic>h</jats:italic> was consistently highly expressed (up to 30-fold) in the transgenic grain. Transgenic lines transformed with the B <jats:sub>1</jats:sub> -hordein promoter with a signal peptide sequence produced a higher level of wheat thioredoxin <jats:italic>h</jats:italic> on average than those without a signal sequence. The overexpression of thioredoxin <jats:italic>h</jats:italic> in the endosperm of germinated grain effected up to a 4-fold increase in the activity of the starch debranching enzyme, pullulanase (limit dextrinase), the enzyme that specifically cleaves α-1,6 linkages in starch. These results raise the question of how thioredoxin <jats:italic>h</jats:italic> enhances the activity of pullulanase because it was found that the inhibitor had become inactive before the enzyme showed appreciable activity. </jats:p>
  • Access State: Open Access