Molecular and biochemical characterisation of polyphenol oxidases in developing kernels and senescing leaves of wheat (Triticum aestivum)
Aravind K. Jukanti A , Phil L. Bruckner A and Andreas M. Fischer A BA Department of Plant Sciences and Plant Pathology, 119AgBioScience Facility, Montana State University, Bozeman, MT 59717-3150, USA.
B Corresponding author. Email: fischer@montana.edu
Functional Plant Biology 33(7) 685-696 https://doi.org/10.1071/FP06050
Submitted: 8 March 2006 Accepted: 2 May 2006 Published: 3 July 2006
Abstract
Polyphenol oxidases (PPOs) have been implicated in plant defence reactions. From an applied point of view, high PPO activity is associated with browning / darkening of fresh and processed food. Owing to its complex genome and economic importance, wheat (Triticum aestivum L.) represents an interesting system to advance our understanding of plant PPO function. We have previously shown that wheat PPOs are organised in a multigene family, consisting of two distinct phylogenetic clusters with three members each. In this study, we demonstrate that members of one cluster are not expressed in developing kernels or senescing flag leaves. Transcriptional regulation of one major gene in the other cluster largely controls PPO levels in these tissues, at least in the wheat varieties used for this study. Our data further indicate that the product of this gene is present as a latent enzyme during early kernel development, and that the latent enzyme is activated during later developmental phases. Enzyme activation can be achieved in vitro by limited tryptic digestion, but our data do not indicate activation by a proteolytic mechanism in vivo. Together, results presented in this study provide important insights into the regulation of wheat PPO function.
Keywords: enzyme activation, partial proteolysis, polyphenol oxidase, Triticum aestivum, wheat.
Acknowledgments
This project was supported by the Montana Agricultural Experiment Station. The authors are thankful to Drs R Wilkinson and M Teintze (Department of Chemistry and Biochemistry, Montana State University) for expert help with mass spectrometric analysis of purified PPO proteins.
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