Titre du document / Document title

A Selaginella lepidophylla trehalose-6-phosphate synthase complements growth and stress-tolerance defects in a yeast tps1 mutant

Auteur(s) / Author(s)

ZENTELLA R. ⁽¹⁾ ; MASCORRO-GALLARDO J. O. ⁽¹⁾ ; VAN DIJCK P. ⁽²⁾ ; FOLCH-MALLOL J. ⁽¹⁾ ; BONINI B. ⁽²⁾ ; VAN VAECK C. ⁽²⁾ ; GAXIOLA R. ⁽¹⁾ ; COVARRUBIAS A. A. ⁽¹⁾ ; NIETO-SOTELO J. ⁽¹⁾ ; THEVELEIN J. M. ⁽²⁾ ; ITURRIAGA G. ⁽¹⁾ ;

Affiliation(s) du ou des auteurs / Author(s) Affiliation(s)

⁽¹⁾ Departamento de Biologia Molecular de Plantas, Instituto de Biotecnologia-Universidad Nacional Autónoma de México, Avenida Universidad 2001, Colonia Chamilpa, 62210 Cuernavaca Morelos, Mexico, MEXIQUE
⁽²⁾ Laboratorium voor Moleculaire Celbiologie and Vlaams Interuniversitair Instituut voor Biotechnologie, Katholieke Universiteit Leuven, Kardinaal Mercierlaan 92, 3001 Leuven-Heverlee, Flanders, BELGIQUE

Résumé / Abstract

The accumulation of the disaccharide trehalose in anhydrobiotic organisms allows them to survive severe environmental stress. A plant cDNA, SITPS1, encoding a 109-kD protein, was isolated from the resurrection plant Selaginella lepidophylla, which accumulates high levels of trehalose. Protein-sequence comparison showed that SITPS1 shares high similarity to trehalose-6-phosphate synthase genes from prokaryotes and eukaryotes. SITPS1 mRNA was constitutively expressed in S. lepidophylla. DNA gel-blot analysis indicated that SITPS1 is present as a single-copy gene. Transformation of a Saccharomyces cerevisiae tps1Δ mutant disrupted in the ScTPS1 gene with S. lepidophylla SITPS1 restored growth on fermentable sugars and the synthesis of trehalose at high levels. Moreover, the SITPS1 gene introduced into the tps1Δ mutant was able to complement both deficiencies: sensitivity to sublethal heat treatment at 39°C and induced thermotolerance at 50°C. The osmosensitive phenotype of the yeast tps1Δ mutant grown in NaCI and sorbitol was also restored by the SITPS1 gene. Thus, SITPS1 protein is a functional plant homolog capable of sustaining trehalose biosynthesis and could play a major role in stress tolerance in S. lepidophylla.

Revue / Journal Title

Plant physiology   ISSN 0032-0889   CODEN PPHYA5 

Source / Source

1999, vol. 119, n^o4, pp. 1473-1482 (1 p.1/4)

Langue / Language

Anglais

Editeur / Publisher

American Society of Plant Physiologists, Rockville, MD, ETATS-UNIS  (1926) (Revue)

Mots-clés anglais / English Keywords

Trehalose ; Biological accumulation ; Tolerance ; Stress ; Complementary DNA ; Sequencing ; Homology ; Synthase ; Gene expression ; Saccharomyces cerevisiae ; Gene ; Mutation ; Complementation ; Biosynthesis ; Enzyme ; Ascomycetes ; Fungi ; Thallophyta ; Pteridophyta ;

Mots-clés français / French Keywords

Tréhalose ; Accumulation biologique ; Tolérance ; Stress ; DNA complémentaire ; Séquençage ; Homologie ; Synthase ; Expression génique ; Saccharomyces cerevisiae ; Gène ; Mutation ; Complémentation ; Biosynthèse ; Gène SlTPS1 ; Trehalose-6-phosphate synthase ; Selaginella lepidophylla ; Enzyme ; Ascomycetes ; Fungi ; Thallophyta ; Pteridophyta ;

Mots-clés espagnols / Spanish Keywords

Trehalosa ; Acumulación biológica ; Tolerancia ; Stress ; DNA complementario ; Sequencing ; Homología ; Synthase ; Expresión genética ; Saccharomyces cerevisiae ; Gen ; Mutación ; Complementación ; Biosíntesis ; Enzima ; Ascomycetes ; Fungi ; Thallophyta ; Pteridophyta ;

Localisation / Location

INIST-CNRS, Cote INIST : 3000, 35400008355233.0350