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Differential expression of alkaline and neutral invertases in response to environmental stresses: characterization of an alkaline isoform as a stress-response enzyme in wheat leaves

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Abstract

It is well accepted that sucrose (Suc) metabolism is involved in responses to environmental stresses in many plant species. In the present study we showed that alkaline invertase (A-Inv) expression is up-regulated in wheat leaves after an osmotic stress or a low-temperature treatment. We demonstrated that the increase of total alkaline/neutral Inv activity in wheat leaves after a stress could be due to the induction of an A-Inv isoform. Also, we identified and functionally characterized the first wheat cDNA sequence that codes for an A-Inv. The wheat leaf full-length sequence encoded a protein 70% similar to a neutral Inv of Lolium temulentum; however, after functional characterization, it resulted to encode a protein that hydrolyzed Suc to hexoses with an optimum pH of 8, and, consequently, the encoding sequence was named Ta-A-Inv. By RT-PCR assays we demonstrated that Ta-A-Inv expression is induced in response to osmotic and cold stress in mature primary wheat leaves. We propose that Ta-A-Inv activity could play an important role associated with a more efficient cytosolic Suc hydrolysis during environmental stresses.

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Abbreviations

A-Inv:

Alkaline invertase

Ac-Inv:

Acid invertase

A/N-Inv:

Alkaline/neutral invertase

An-:

Anabaena

FSE:

Fructan synthesis enzymes

N-Inv:

Neutral invertase

RS:

Reducing sugars

Suc:

Sucrose

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Acknowledgments

We are grateful to Clara Fernández for technical assistance and our colleagues at the Centro de Investigaciones Biológicas for helpful discussions. This work is part of the PhD thesis of WAV, Universidad Nacional de Mar del Plata (UNMdP), Argentina. Supported by Agencia Nacional de Promoción Científica y Tecnológica (ANPCyT), Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET, PID 6105), and UNMdP.

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  1. Walter A. Vargas

    Present address: Department of Plant Pathology and Microbiology, Texas A&M University, College Station, TX, 77843, USA

Authors and Affiliations

  1. Centro de Investigaciones Biológicas, Fundación para Investigaciones Biológicas Aplicadas (FIBA), C.C. 1348, 7600, Mar del Plata, Argentina

    Walter A. Vargas, Horacio G. Pontis & Graciela L. Salerno

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  1. Walter A. Vargas
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  2. Horacio G. Pontis
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  3. Graciela L. Salerno
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Correspondence to Graciela L. Salerno.

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425_2007_590_MOESM1_ESM.tif

Fig. S1 Alignment of deduced amino-acid sequences of wheat A/N-Inv and previously characterized A/N-Inv. Sequence alignments of T. aestivum A/N-Inv-like (named as Ta-A-Inv after functional characterization, accession number AM295169), D. carota N-Inv (Dc-N-Inv Y16262), L. temulentum N-Inv (Lt-N-Inv AP003143), A. thaliana A-Inv (CNIV1, At1g35580), O. sativa A/N-Inv (OsNIN1, AK103334) and Anabaena sp. PCC 7120 A-Inv and N-Inv (An-InvA, AJ491788, and An-InvB, AJ311089). The three regions described by Sturm et al. (1999) for the identification of protein function are indicated as 1, 2 and 3 on the right. Residue numbers for amino acids are shown on the left. Residues present in the five sequences are shaded in grey, residues conserved only in Ta-A/N-Inv-like, CNIV1 and An-InvA are black shaded (TIF 17711 kb).

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Vargas, W.A., Pontis, H.G. & Salerno, G.L. Differential expression of alkaline and neutral invertases in response to environmental stresses: characterization of an alkaline isoform as a stress-response enzyme in wheat leaves. Planta 226, 1535–1545 (2007). https://doi.org/10.1007/s00425-007-0590-3

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