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Molecular characterization of glyoxalase-I from a higher plant; upregulation by stress

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Abstract

A cDNA, GLX1, encoding glyoxalase-I was isolated by differential screening of salt-induced genes in tomato. Glyoxalases-I and-II are ubiquitous enzymes whose functions are not clearly understood. They may serve to detoxify methylglyoxal produced from triosephosphates in all cells. The protein encoded by GLX1 shared 49.4% and 58.5% identity with glyoxalase-I isolated from bacteria and human, respectively. Furthermore, yeast cells expressing GLX1 showed a glyoxalase-I specific activity 20-fold higher than non-transformed cells. Both GLX1 mRNA and glyoxalase-I polypeptide levels increased 2- to 3-fold in roots, stems and leaves of plants treated with either NaCl, mannitol, or abscisic acid. Immunohistochemical localization indicated that glyoxalase-I was expressed in all cell types, with preferential accumulation in phloem sieve elements. This expression pattern was not appreciably altered by salt-stress. We suggest that the increased expression of glyoxalase-I may be linked to a higher demand for ATP generation and to enhanced glycolysis in salt-stressed plants.

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Authors and Affiliations

  1. Instituto de Recursos Naturales y Agrobiología, C.S.I.C., Apdo. 1052, 41080, Sevilla, Spain

    Joaquín Espartero & José M. Pardo

  2. Departamento de Biología Celular, Facultad de Biología, Universidad de Sevilla, 41012, Sevilla, Spain

    Inmaculada Sánchez-Aguayo

Authors
  1. Joaquín Espartero
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  2. Inmaculada Sánchez-Aguayo
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  3. José M. Pardo
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Espartero, J., Sánchez-Aguayo, I. & Pardo, J.M. Molecular characterization of glyoxalase-I from a higher plant; upregulation by stress. Plant Mol Biol 29, 1223–1233 (1995). https://doi.org/10.1007/BF00020464

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