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Abstract <p>Thioredoxins (TRXs) are small, conserved redox-active proteins that play central roles in oxidative stress responses. Here, we identified and functionally characterized a novel thioredoxin, <i>MpTRX1</i>, from the newly isolated yeast <i>Metschnikowia persimmonesis</i>. The full-length <i>MpTRX1</i> gene was cloned and expressed in <i>Escherichia coli</i> and <i>Saccharomyces cerevisiae</i> to analyze its biochemical and physiological functions. <i>MpTRX1</i> encodes a 103-amino-acid protein containing a canonical CXXC redox motif, and structural modeling confirmed a conserved thioredoxin fold. Recombinant <i>MpTRX1</i> exhibited clear disulfide reductase activity in both DTNB (5,5′-dithiobis-(2-nitrobenzoic acid)) and insulin reduction assays. Mutation of either catalytic cysteine residue abolished activity, confirming their essential roles. Moreover, heterologous expression of <i>MpTRX1</i> in <i>S. cerevisiae</i> enhanced tolerance to hydrogen-peroxide-induced oxidative stress<b>.</b> Although the functional assays were conducted in a heterologous system, these findings demonstrate that <i>MpTRX1</i> is a bona fide thioredoxin that may contribute to oxidative stress protection in <i>M. persimmonesis</i>. This work provides the first molecular characterization of a protein from <i>M. persimmonesis</i> and establishes a foundation for future studies on its potential ecological and biotechnological applications.</p> Key points <p><i>• Identification of MpTRX1, a novel thioredoxin from M. persimmonesis</i>.</p> <p><i>• Recombinant MpTRX1 reduces both chemical and protein substrates</i>.</p> <p><i>• Overexpression of MpTRX1 enhances oxidative stress tolerance in S. cerevisiae</i>.</p> Graphical Abstract <p></p>

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Identification and functional characterization of a novel thioredoxin MpTRX1 from Metschnikowia persimmonesis

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年12月23日

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  • Chang Ho Kang,
  • Jae Hyeok Lee,
  • Yeong Min Lee,
  • Yong Bok Lee,
  • Youngmin Kang,
  • Yeongjun Ban,
  • Ariranur Haniffadli,
  • Endang Rahmat,
  • Chae Oh Lim

摘要

Abstract

Thioredoxins (TRXs) are small, conserved redox-active proteins that play central roles in oxidative stress responses. Here, we identified and functionally characterized a novel thioredoxin, MpTRX1, from the newly isolated yeast Metschnikowia persimmonesis. The full-length MpTRX1 gene was cloned and expressed in Escherichia coli and Saccharomyces cerevisiae to analyze its biochemical and physiological functions. MpTRX1 encodes a 103-amino-acid protein containing a canonical CXXC redox motif, and structural modeling confirmed a conserved thioredoxin fold. Recombinant MpTRX1 exhibited clear disulfide reductase activity in both DTNB (5,5′-dithiobis-(2-nitrobenzoic acid)) and insulin reduction assays. Mutation of either catalytic cysteine residue abolished activity, confirming their essential roles. Moreover, heterologous expression of MpTRX1 in S. cerevisiae enhanced tolerance to hydrogen-peroxide-induced oxidative stress. Although the functional assays were conducted in a heterologous system, these findings demonstrate that MpTRX1 is a bona fide thioredoxin that may contribute to oxidative stress protection in M. persimmonesis. This work provides the first molecular characterization of a protein from M. persimmonesis and establishes a foundation for future studies on its potential ecological and biotechnological applications.

Key points

• Identification of MpTRX1, a novel thioredoxin from M. persimmonesis.

• Recombinant MpTRX1 reduces both chemical and protein substrates.

• Overexpression of MpTRX1 enhances oxidative stress tolerance in S. cerevisiae.

Graphical Abstract