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<p>Nitrate transporter NRT1.1 plays a central role in nitrogen (N) assimilation in <i>Arabidopsis thaliana</i> (Arabidopsis), functioning as both a dual-affinity transporter and a nitrate sensor. However, the functional conservation of NRT1.1 orthologs in crops remains to be fully elucidated. Here, we characterized BrNPF6.6, a close homolog of NRT1.1 in <i>Brassica rapa</i>. Subcellular localization confirmed its plasma membrane localization, consistent with a role in nitrate transport. Expression analysis revealed tissue-specific responses to nitrate availability, with leaf <i>BrNPF6.6</i> transcripts peaking under low N conditions. Functional complementation assays in the Arabidopsis <i>chl1-5</i> mutant demonstrated that BrNPF6.6 restores nitrate accumulation, represses <i>NRT2.1/2.4/2.5</i> expression under N-sufficient conditions, and partially complements the lateral root phenotype in <i>chl1-5</i> mutant under low N conditions. These findings support that BrNPF6.6 is a close homolog of NRT1.1, highlighting the conservation of NRT1.1-mediated N assimilation functions.</p>

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Characterization of BrNPF6.6 in Brassica rapa Reveals the Conservation of Nitrate Transporter 1.1

  • 期刊论文

  • 发表日期：

    2026年7月3日

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  • Jia Wang,
  • Zeneng Wang,
  • Mengyun Wang,
  • Yuqing Wang,
  • Yibo Teng

摘要

Nitrate transporter NRT1.1 plays a central role in nitrogen (N) assimilation in Arabidopsis thaliana (Arabidopsis), functioning as both a dual-affinity transporter and a nitrate sensor. However, the functional conservation of NRT1.1 orthologs in crops remains to be fully elucidated. Here, we characterized BrNPF6.6, a close homolog of NRT1.1 in Brassica rapa. Subcellular localization confirmed its plasma membrane localization, consistent with a role in nitrate transport. Expression analysis revealed tissue-specific responses to nitrate availability, with leaf BrNPF6.6 transcripts peaking under low N conditions. Functional complementation assays in the Arabidopsis chl1-5 mutant demonstrated that BrNPF6.6 restores nitrate accumulation, represses NRT2.1/2.4/2.5 expression under N-sufficient conditions, and partially complements the lateral root phenotype in chl1-5 mutant under low N conditions. These findings support that BrNPF6.6 is a close homolog of NRT1.1, highlighting the conservation of NRT1.1-mediated N assimilation functions.