| Thioredoxins are a class of redox regulatory proteins that are widely present in plants and play crucial roles in plant growth and development. To investigate the biological functions of the wheat thioredoxin TaTrxh10, we systematically analyzed its sequence characteristics, three-dimensional structure, and gene expression patterns. Additionally, the protein was expressed in a prokaryotic system, and its disulfide bond reduction activity was validated in vitro. Sequence analysis revealed that wheat TaTrxh10 comprises three family members encoded by three homoeologous genes: TaTrxh10-A, TaTrxh10-B, and TaTrxh10-D. All three TaTrxh10 family members consist of 143 amino acids, with a sequence identity of 94.4%, and contain the classic thioredoxin conserved domain and catalytic active center (WCGPC). Protein structural analysis demonstrated that TaTrxh10 can fold into a sandwich-like spatial structure composed of five β-sheets and four α-helices. Gene expression analysis indicated that the three homoeologous genes of TaTrxh10 are expressed at very low levels in roots, stems, and leaves, and at relatively lower levels in the ovary and mature seeds; however, they are highly expressed in mature pollens. The thioredoxin reduction activity assay using DTNB demonstrated that all three family members of TaTrxh10 possess the ability to catalyze disulfide bond reduction, although their reduction activities varied among the members. In reaction systems with lower thioredoxin concentrations, TaTrxh10-D exhibited the highest catalytic activity, followed by TaTrxh10-B. These results indicate that wheat TaTrxh10 represents a class of active redox regulatory proteins specifically expressed in pollen, providing important insights for further exploration of redox-dependent developmental regulatory mechanisms in wheat. |
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