Plant Molecular Biology

, Volume 29, Issue 6, pp 1223–1233

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

  • Joaquín Espartero
  • Inmaculada Sánchez-Aguayo
  • José M. Pardo
Research article

DOI: 10.1007/BF00020464

Cite this article as:
Espartero, J., Sánchez-Aguayo, I. & Pardo, J.M. Plant Mol Biol (1995) 29: 1223. doi:10.1007/BF00020464

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.

Key words

expression pattern glyoxalase-I Lycopersicon esculentum phloem sequence salt-stress 

Copyright information

© Kluwer Academic Publishers 1995

Authors and Affiliations

  • Joaquín Espartero
    • 1
  • Inmaculada Sánchez-Aguayo
    • 2
  • José M. Pardo
    • 1
  1. 1.Instituto de Recursos Naturales y AgrobiologíaC.S.I.C.SevillaSpain
  2. 2.Departamento de Biología Celular, Facultad de BiologíaUniversidad de SevillaSevillaSpain

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