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<p>Sensory rhodopsins (SRs) in haloarchaea form complexes with their cognate transducers (Htrs) to produce wavelength-specific phototactic responses, yet similar architectures mediate distinct behaviors: SRI mediates attraction, SRII drives repulsion, whereas SRM modulates both responses. Until now, structural insight was limited to the <i>Natronomonas pharaonis</i> SRII-HtrII system in a truncated form, without a full-length counterpart for comparison. Moreover, NpHtrII is distinct among HtrII transducers in lacking the large periplasmic domain retained in homologs from <i>Halobacterium salinarum</i>, <i>Haloarcula marismortui</i> and <i>Haloarcula taiwanensis</i>, leaving the canonical SR-Htr architecture unknown. Here, we report the cryo-EM structure of the <i>Haloarcula taiwanensis</i> SRI-HtrI complex, providing a near native, non-crystallized view of a full-length SR-Htr dimer with the cytoplasmic HAMP1 domain resolved. The structure reveals the intact homodimeric receptor-transducer assembly and visualizes the interface between the helix G (Arg215), SRI E-F loop (Pro154), and HtrI HAMP1. These findings fill the long-standing structural gap for a canonical SR-Htr complex and establish a framework for conserved receptor-transducer coupling across archaeal phototaxis systems.</p>

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Cryo-EM structure of the SRI-HtrI complex reveals the cytoplasmic coupling in an archaeal phototaxis system

  • 期刊论文

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  • 发表日期：

    2026年4月16日

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  • Guo Zhen Lim,
  • Yu-En Lin,
  • Pei-Chun Chen,
  • Hsu-Yuan Fu,
  • Chii-Shen Yang

摘要

Sensory rhodopsins (SRs) in haloarchaea form complexes with their cognate transducers (Htrs) to produce wavelength-specific phototactic responses, yet similar architectures mediate distinct behaviors: SRI mediates attraction, SRII drives repulsion, whereas SRM modulates both responses. Until now, structural insight was limited to the Natronomonas pharaonis SRII-HtrII system in a truncated form, without a full-length counterpart for comparison. Moreover, NpHtrII is distinct among HtrII transducers in lacking the large periplasmic domain retained in homologs from Halobacterium salinarum, Haloarcula marismortui and Haloarcula taiwanensis, leaving the canonical SR-Htr architecture unknown. Here, we report the cryo-EM structure of the Haloarcula taiwanensis SRI-HtrI complex, providing a near native, non-crystallized view of a full-length SR-Htr dimer with the cytoplasmic HAMP1 domain resolved. The structure reveals the intact homodimeric receptor-transducer assembly and visualizes the interface between the helix G (Arg215), SRI E-F loop (Pro154), and HtrI HAMP1. These findings fill the long-standing structural gap for a canonical SR-Htr complex and establish a framework for conserved receptor-transducer coupling across archaeal phototaxis systems.