Zinc finger domains bind low-complexity domain polymers
N. Iguchi, N. Isozumi, Y. Hattori, T. Imamura, M. So, H. Nanaura, T. Kiriyama, N. Eura, M. Yamaoka, M. Nakanishi, M. Mori, S. Ohki, H. Kumeta, H. Koga, M. Watabe, T. Mabuchi, S. Kanemura, M. Okumura, T. Yoshizawa, I. Ota, N. Suzuki, M. Aoki, Y. Yamashiro, T. Saio, K. Sugie, E. Mori
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-{beta} 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.
02 /Specification & Classification
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