Molecular insights into RNA recognition by the ZAR1 C-terminal domain.

Authors

Qingling Liu, Haoyu Ma, Xian He, Chao Xu, Jiahai Zhang

Published in

FEBS letters. May 19, 2025. Epub May 19, 2025.

Abstract

Zygote arrested-1 (ZAR1)-dependent translational repression plays an important role during early oogenesis. Here, we solved the crystal structure of the C-terminal domain of ZAR1, which contains three zinc-binding motifs, and confirmed its ability to bind to RNAs derived from translation control sequence elements within the 3'-UTRs of Wee1 and Mos mRNAs. By using the AlphaFold server, we obtained a predicted model for the structure of the ZAR1 C-terminal domain bound with a 13-nt RNA. Mutagenesis and biochemistry experiments further validated the ZAR1-RNA interaction. Therefore, our study provides insights into RNA recognition by the ZAR1 zinc-binding domain and the role of ZAR1 in repressing gene expression. Impact statement Zygote arrested-1 (ZAR1)-dependent translational repression finely orchestrates gene expression during early oogenesis. Here, we solved the high-resolution structure of the C-terminal zinc-binding domain of ZAR1 and confirmed its binding to RNA. The modeled ZAR1-RNA complex by Alphafold further provides insight into RNA recognition by ZAR1.

PMID:
40388637
Bibliographic data and abstract were imported from PubMed on 20 May 2025.

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