Zinc finger domains bind low-complexity domain polymers

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.

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Publication Details

Journal
Nature Communications
Published
2025-10-16
DOI
https://doi.org/10.1038/s41467-025-64382-2
Primary Topic
RNA Research and Splicing
Type
article
Field-Weighted Citation Impact
0.00

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article

Zinc finger domains bind low-complexity domain polymers

Mari Nakanishi, Yoshikazu Hattori, Fumika Ide, Nobuyuki Eura et al.
Nature Communications
RNA Research and Splicing
article

Zinc finger domains bind low-complexity domain polymers

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

Abstract

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.

Nature CommunicationsVol. 16(1)
Ritsumeikan University (JP), Japan Advanced Institute of Science and Technology (JP), Ishikawa Prefectural University (JP), Tohoku University (JP), Hokkaido University (JP), Kyoto University (JP), National Cerebral and Cardiovascular Center (JP), Nara Medical University Hospital (JP), Nara Medical University (JP), Kindai University (JP), Tokushima University (JP)
Nakatomi Foundation, Japan Agency for Medical Research and Development, National Institute of Advanced Industrial Science and Technology, Kanazawa University, Ministry of Education, Culture, Sports, Science and Technology, Kato Memorial Bioscience Foundation, Hokkaido University, SENSHIN Medical Research Foundation, Japan Society for the Promotion of Science
Openalex Percentile: Top 74%
RNA Research and Splicing
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