Abstract

Wheat (Triticum aestivum L.) seedlings contain four alanine aminotransferase (AlaAT) homologues. Two of them encode AlaAT enzymes, whereas two homologues act as glumate:glyoxylate aminotransferase (GGAT). To address the function of the distinct AlaAT homologues a comparative examination of the changes in transcript level together with the enzyme activity and alanine and glutamate content in wheat seedlings subjected to low oxygen availability, nitrogen and light deficiency has been studied. Shoots of wheat seedlings were more tolerant to hypoxia than the roots as judging on the basis of enzyme activity and transcript level. Hypoxia induced AlaAT1 earlier in roots than in shoots, while AlaAT2 and GGAT were unaffected. The increase in AlaAT activity lagged behind the increase in alanine content. Nitrogen deficiency has little effect on the activity of GGAT. In contrast, lower activity of AlaAT and the level of mRNA for AlaAT1 and AlaAT2 in wheat seedlings growing on a nitrogen-free medium seems to indicate that AlaAT is regulated by the availability of nitrogen. Both AlaAT and GGAT activities were present in etiolated wheat seedlings but their activity was half of that observed in light-grown seedlings. Exposure of etiolated seedlings to light caused an increase in enzyme activities and up-regulated GGAT1. It is proposed that hypoxia-induced AlaAT1 and light-induced peroxisomal GGAT1 appears to be crucial for the regulation of energy availability in plants grown under unfavourable environmental conditions. Key message In young wheat seedlings, both AlaAT and GGAT are down-regulated by nitrogen deficiency, whereas AlaAT1 is upregulated by hypoxia and GGAT1 by light.

Highlights

  • Alanine aminotransferase (AlaAT) catalyses the reversible reaction of conversion of alanine and 2–oxoglutarate into pyruvate and glutamate

  • A phylogenetic analysis of alanine aminotransferase (AlaAT) from Arabidopsis thaliana and Triticum aestivum performed using ClustalW programme (Higgins et al 1994) showed that two of them were closely related to Arabidopsis AlaAT1 and AlaAT2 while other two appeared to be related to GGAT1 and GGAT2 (Fig. 2b)

  • The results presented here indicate that in wheat seedlings four alanine aminotransferase homologues are present

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Summary

Introduction

Alanine aminotransferase (AlaAT) catalyses the reversible reaction of conversion of alanine and 2–oxoglutarate into pyruvate and glutamate. It was suggested that AlaAT is involved in degradation of alanine after low oxygen stress relief This finding has been confirmed by Miyashita et al (2007) who showed that the Arabidopsis AlaAT1 knock-out mutant (alaat1-1) was able to accumulate more alanine during hypoxia than wild type plants and the decline in accumulated alanine was delayed during recovery period. It appears that AlaAT plays limited role in alanine synthesis under low oxygen conditions, while elevated levels of AlaAT activity enables to convert rapidly the accumulated alanine back into pyruvate during recovery phase (Miyashita et al 2007). Photosynthesis genes are expressed in the later phase of growth (Jang and Sheen 1994; Loza-Tavera et al 1990)

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