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<p>The UV-B photoreceptor UVR8 plays a central role in plant responses to ultraviolet light, but its function in extremophilic algae remains poorly understood. In this study, we isolated and characterized a UVR8 homolog (<i>CiUVR8</i>) from the Antarctic ice alga <i>Chlamydomonas</i> sp. ICE-L. The full-length <i>CiUVR8</i> gene encodes a 406-amino-acid protein highly conserved with <i>Arabidopsis thaliana</i> UVR8, including the key tryptophan residues essential for UV-B perception. Bioinformatics and phylogenetic analyses confirmed its structural conservation and distinct evolutionary placement among polar algae. Quantitative real-time PCR revealed that <i>CiUVR8</i> expression is dynamically regulated in response to temperature (-20&#xa0;°C to 15&#xa0;°C), salinity (16‰ to 128‰), and varying intensities of UV-B radiation. Notably, <i>CiUVR8</i> expression generally decreased with increasing UV-B intensity, suggesting a potential photoprotective mechanism. The recombinant CiUVR8 protein was successfully expressed in <i>Escherichia coli</i> and purified, providing a foundation for subsequent functional validation. These results highlight CiUVR8 as a functional UV-B receptor involved in stress adaptation, offering insight into algal survival strategies in extreme polar environments.</p>

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Molecular cloning and expression analysis of the ultraviolet-B (UV-B) photoreceptor UVR8 in the Antarctic ice Alga Chlamydomonas sp. ICE-L

  • 期刊论文

  • 发表日期：

    2025年12月8日

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  • Xinning Pan,
  • Zhou Zheng,
  • Zhiru Liu,
  • Yanan Tan,
  • Ning Du

摘要

The UV-B photoreceptor UVR8 plays a central role in plant responses to ultraviolet light, but its function in extremophilic algae remains poorly understood. In this study, we isolated and characterized a UVR8 homolog (CiUVR8) from the Antarctic ice alga Chlamydomonas sp. ICE-L. The full-length CiUVR8 gene encodes a 406-amino-acid protein highly conserved with Arabidopsis thaliana UVR8, including the key tryptophan residues essential for UV-B perception. Bioinformatics and phylogenetic analyses confirmed its structural conservation and distinct evolutionary placement among polar algae. Quantitative real-time PCR revealed that CiUVR8 expression is dynamically regulated in response to temperature (-20 °C to 15 °C), salinity (16‰ to 128‰), and varying intensities of UV-B radiation. Notably, CiUVR8 expression generally decreased with increasing UV-B intensity, suggesting a potential photoprotective mechanism. The recombinant CiUVR8 protein was successfully expressed in Escherichia coli and purified, providing a foundation for subsequent functional validation. These results highlight CiUVR8 as a functional UV-B receptor involved in stress adaptation, offering insight into algal survival strategies in extreme polar environments.