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Published on December 27, 2007; 10.1104/pp.107.113639

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Received November 21, 2007
Accepted December 12, 2007

The NADPH-dependent thioredoxin reductase/thioredoxin system in germinating barley seeds: gene expression, protein profiles and interactions between isoforms of thioredoxin h and thioredoxin reductase

Azar Shahpiri , Birte Svensson , and Christine Finnie *

Enzyme and Protein Chemistry, BioCentrum-DTU, Technical University of Denmark, Soltofts Plads, Building 224, DK-2800 Kgs. Lyngby, Denmark

* Corresponding author; email: csf{at}biocentrum.dtu.dk.

The NADPH-dependent thioredoxin reductase (NTR)/thioredoxin (Trx) system catalyses disulphide bond reduction in the cytoplasm and mitochondrion. Trx h is suggested to play important roles in seed development, germination and seedling growth. Plants have multiple isoforms of Trx h and NTR, however, little is known about the roles of the individual isoforms. Trx h isoforms from barley seeds (HvTrxh1 and HvTrxh2) were characterized previously. In the present study two NTR isoforms (HvNTR1 and HvNTR2) were identified, enabling comparison of gene expression, protein appearance and interaction between individual NTR and Trx h isoforms in barley embryo and aleurone layers. Although mRNA encoding both Trx h isoforms is present in embryo and aleurone layer, the corresponding proteins differed in spatio-temporal appearance. HvNTR2, but not HvNTR1 gene expression seems to be regulated by gibberellic acid. Recombinant HvNTR1 and HvNTR2 exhibited virtually the same affinity towards HvTrxh1 and HvTrxh2, whereas HvNTR2 has slightly higher catalytic activity than HvNTR1 with both Trx h isoforms, and HvNTR1 has slightly higher catalytic activity towards HvTrxh1 than HvTrxh2. Notably, both NTRs reduced Trx h at the acidic conditions residing in the starchy endosperm during germination. Interspecies reactions between the barley proteins and E. coli Trx or Arabidopsis thaliana NTR, respectively, occurred with 20-90 fold weaker affinity. This first investigation of regulation and interactions between members of the NTR/Trx system in barley seed tissues suggests that different isoforms are differentially regulated but may have overlapping roles, with HvNTR2 and HvTrxh1 being the predominant isoforms in aleurone layer.




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