Journal Article

Expression of Mangrove Allene Oxide Cyclase Enhances Salt Tolerance in <i>Escherichia coli</i>, Yeast, and Tobacco Cells

Akiyo Yamada, Takeo Saitoh, Tetsuro Mimura and Yoshihiro Ozeki

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 43, issue 8, pages 903-910
Published in print August 2002 | ISSN: 0032-0781
Published online August 2002 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/pcp/pcf108
Expression of Mangrove Allene Oxide Cyclase Enhances Salt Tolerance in Escherichia coli, Yeast, and Tobacco Cells

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  • Molecular and Cell Biology
  • Plant Sciences and Forestry

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To analyze the mechanisms of salt tolerance in the mangrove plant, Bruguiera sexangula, functional screening for cDNAs encoding proteins essential for salt tolerance was performed using Escherichia coli as the host organism. A transformant expressing a protein homologous to Lycopersicon (tomato) allene oxide cyclase (AOC) displayed enhanced salt tolerance. However, this unusual trait is not conferred by Lycopersicon AOC or its Arabidopsis homolog. Analysis of the functional region revealed a sequence of only 70 amino acids, which contains an unusual sequence that is essential for the salt-tolerant phenotype. On the basis of its unusual function, the mangrove AOC homolog is designated “mangrin”. Furthermore, expression of mangrin driven by the GAL1 promoter and the 35S cauliflower mosaic virus (CaMV) promoter in Saccharomyces cerevisiae and tobacco cell lines, respectively, also gave rise to enhanced salt tolerance. Mangrin transcripts increased in cultured B. sexangula cells in response to salt stress. We propose that mangrin plays an important role in the salt-tolerance mechanism of B. sexangula, and that the biosynthesis of mangrin might be an effective means of enhancing salt tolerance in higher plants.

Keywords: Keywords: Mangrove — Bruguiera sexangula — Salt-tolerance.; Abbreviations: 35S CaMV promoter, 35S cauliflower mosaic virus promoter; AOC, allene oxide cyclase; GUS, β-glucuronidase.

Journal Article.  4314 words.  Illustrated.

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

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