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J Exp Bot. 2007;58(15-16):4365-72. doi: 10.1093/jxb/erm303.

Different regulation of haloperoxidation during agar oligosaccharide-activated defence mechanisms in two related red algae, Gracilaria sp. and Gracilaria chilensis.

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1
Station Biologique, UMR 7139 CNRS-UPMC and LIA DIAMS, BP74, F-29682 Roscoff, France. fweinberger@fm-geomar.de

Abstract

The related red seaweeds Gracilaria sp. from the eastern Mediterranean and Gracilaria chilensis from Chile were similar in their enzymatic inventory for halogenation. In both species, halogenation was dependent upon H(2)O(2) and thus driven by haloperoxidases. These could be inhibited with phosphate and reversibly inhibited with azide and were therefore apparently dependent upon vanadate. Both species generated in the first line bromoform and other brominated halocarbons. Gel electrophoresis under non-denaturating conditions demonstrated that both species expressed halogenating peroxidases. Elicitation of Gracilaria sp. with agar oligosaccharides resulted in marked increases in bromination, iodination, and chlorination. Production rates of volatile halocarbons and phenol red bromination both increased by a factor of eight, presumably due to increased availability for haloperoxidases of H(2)O(2) during the oxidative burst response. Elicitation of Gracilaria sp. also triggered a release of bromide ions through DIDS-sensitive anion channels, which allowed for some bromination in bromide-free medium. However, this effect was relatively limited. By contrast, agar oligosaccharide oxidation in G. chilensis did not increase halogenation. Obviously, agar oligosaccharide oxidation does not provide sufficient amounts of hypohalous acids for such increases, because it does not deliver H(2)O(2) at the active site of vanadium-dependent haloperoxidases. These results correlate with earlier findings that the agar oligosaccharide-elicited oxidative burst controls microorganisms while agar oligosaccharide oxidation does not.

PMID:
18182438
DOI:
10.1093/jxb/erm303
[Indexed for MEDLINE]
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