Journal Article

Activity of the C-terminal-Dependent Vacuolar Sorting Signal of Horseradish Peroxidase C1a is Enhanced by its Secondary Structure

Takeshi Matsui, Ayako Tabayashi, Megumi Iwano, Atsuhiko Shinmyo, Ko Kato and Hideki Nakayama

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 52, issue 2, pages 413-420
Published in print February 2011 | ISSN: 0032-0781
Published online January 2011 | e-ISSN: 1471-9053 | DOI: https://dx.doi.org/10.1093/pcp/pcq205
Activity of the C-terminal-Dependent Vacuolar Sorting Signal of Horseradish Peroxidase C1a is Enhanced by its Secondary Structure

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  • Biochemistry
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  • Plant Sciences and Forestry

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Plant class III peroxidase (PRX) catalyzes the oxidation and oxidative polymerization of a variety of phenolic compounds while reducing hydrogen peroxide. PRX proteins are classified into apoplast type and vacuole type based on the absence or the presence of C-terminal propeptides, which probably function as vacuolar sorting signals (VSSs). In this study, in order to improve our understanding of vacuole-type PRX, we analyzed regulatory mechanisms of vacuolar sorting of a model vacuole-type PRX, the C1a isozyme of horseradish (Armoracia rusticana) (HRP C1a). Using cultured transgenic tobacco cells and protoplasts derived from horseradish leaves, we characterized HRP C1a’s VSS, which is a 15 amino acid C-terminal propeptide (C15). We found that the C-terminal hexapeptide of C15 (C6), which is well conserved among vacuole-type PRX proteins, forms the core of the C-terminal-dependent VSS. We also found that the function of C6 is enhanced by the remaining N-terminal part of C15 which probably folds into an amphiphilic α-helix.

Keywords: Amphiphilic α-helix; Horseradish peroxidase C1a; Vacuolar sorting signal

Journal Article.  5455 words.  Illustrated.

Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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