Girolline is a sequence context-selective modulator of eIF5A activity

Tilman Schneider-Poetsch (), Yongjun Dang, Wakana Iwasaki, Mayumi Arata, Yuichi Shichino, Ali Al Mourabit, Celine Moriou, Daniel Romo, Jun O. Liu, Takuhiro Ito, Shintaro Iwasaki and Minoru Yoshida ()
Additional contact information
Tilman Schneider-Poetsch: Wako
Yongjun Dang: Chongqing Medical University
Wakana Iwasaki: RIKEN Center for Biosystems Dynamics Research
Mayumi Arata: Wako
Yuichi Shichino: Wako
Ali Al Mourabit: Université Paris-Saclay
Celine Moriou: Université Paris-Saclay
Daniel Romo: One Bear Place
Jun O. Liu: The Johns Hopkins University School of Medicine
Takuhiro Ito: RIKEN Center for Biosystems Dynamics Research
Shintaro Iwasaki: Wako
Minoru Yoshida: Wako

Nature Communications, 2025, vol. 16, issue 1, 1-13

Abstract: Abstract Natural products have a long history of providing probes into protein biosynthesis, with many of these compounds serving as therapeutics. The marine natural product girolline has been described as an inhibitor of protein synthesis. Its precise mechanism of action, however, has remained unknown. The data we present here suggests that girolline is a sequence-selective modulator of translation factor eIF5A. Girolline interferes with ribosome-eIF5A interaction and induces ribosome stalling where translational progress is impeded, including on AAA-encoded lysine. Our data furthermore indicate that eIF5A plays a physiological role in ribosome-associated quality control and in maintaining the efficiency of translational progress. Girolline helped to deepen our understanding of the interplay between protein production and quality control in a physiological setting and offers a potent chemical tool to selectively modulate gene expression.

Date: 2025
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DOI: 10.1038/s41467-024-54838-2

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