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<p>Self-association of low-complexity protein sequences (LC domains) is important for polymer formation. Several molecular chaperones are involved in the regulation of LC domain polymer formation. However, the mechanisms underlying cell recognition of LC domain polymers remain unclear. Here we show that zinc finger domains (ZnFs) bind LC domains of RNA-binding proteins in a cross-β polymer-dependent manner. ZnFs bound to LC domain hydrogels and suppressed LC domain polymer formation. Moreover, ZnFs preferentially recognize LC domains in the polymeric state. These findings suggest that ZnFs act as physiological regulators of LC domain polymer formation.</p>

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Zinc finger domains bind low-complexity domain polymers

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年10月16日

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  • Naohiko Iguchi,
  • Noriyoshi Isozumi,
  • Yoshikazu Hattori,
  • Tomohiro Imamura,
  • Takeshi Yokoyama,
  • Masatomo So,
  • Hitoki Nanaura,
  • Takao Kiriyama,
  • Nobuyuki Eura,
  • Minako Yamaoka,
  • Naoki Iwasa,
  • Tomo Shiota,
  • Mari Nakanishi,
  • Nanako Konishi,
  • Haruka Ito,
  • Akihito Takeuchi,
  • Masashi Mori,
  • Shinya Ohki,
  • Hiroyuki Kumeta,
  • Hironori Koga,
  • Mai Watabe,
  • Takuya Mabuchi,
  • Shingo Kanemura,
  • Masaki Okumura,
  • Yoshikazu Tanaka,
  • Ken Morishima,
  • Masaaki Sugiyama,
  • Fumika Ide,
  • Hiroyoshi Matsumura,
  • Takuya Yoshizawa,
  • Ichiro Ota,
  • Naoki Suzuki,
  • Masashi Aoki,
  • Yoshito Yamashiro,
  • Tomohide Saio,
  • Kazuma Sugie,
  • Eiichiro Mori

摘要

Self-association of low-complexity protein sequences (LC domains) is important for polymer formation. Several molecular chaperones are involved in the regulation of LC domain polymer formation. However, the mechanisms underlying cell recognition of LC domain polymers remain unclear. Here we show that zinc finger domains (ZnFs) bind LC domains of RNA-binding proteins in a cross-β polymer-dependent manner. ZnFs bound to LC domain hydrogels and suppressed LC domain polymer formation. Moreover, ZnFs preferentially recognize LC domains in the polymeric state. These findings suggest that ZnFs act as physiological regulators of LC domain polymer formation.