Author
Listed:
- Naoki Konno
(The University of Tokyo)
- Keita Miyake
(The University of Tokyo)
- Satoshi Nishino
(The University of Tokyo
The University of Tokyo)
- Kimiho Omae
(The University of Tokyo
RIKEN)
- Haruaki Yanagisawa
(The University of Tokyo)
- Saburo Tsuru
(The University of Tokyo)
- Yuki Nishimura
(The University of Tokyo)
- Masahide Kikkawa
(The University of Tokyo)
- Chikara Furusawa
(The University of Tokyo
RIKEN)
- Wataru Iwasaki
(The University of Tokyo
The University of Tokyo)
Abstract
Convergent evolution of proteins provides insights into repeatability of genetic adaptation. While local convergence of proteins at residue or domain level has been characterized, global structural convergence by inter-domain/molecular interactions remains largely unknown. Here we present structural convergent evolution on fusion enzymes of aldehyde dehydrogenases (ALDHs) and alcohol dehydrogenases (ADHs). We discover BdhE (bifunctional dehydrogenase E), an enzyme clade that emerged independently from the previously known AdhE family through distinct gene fusion events. AdhE and BdhE show shared enzymatic activities and non-overlapping phylogenetic distribution, suggesting common functions in different species. Cryo-electron microscopy reveals BdhEs form donut-like homotetramers, contrasting AdhE’s helical homopolymers. Intriguingly, despite distinct quaternary structures and
Suggested Citation
Naoki Konno & Keita Miyake & Satoshi Nishino & Kimiho Omae & Haruaki Yanagisawa & Saburo Tsuru & Yuki Nishimura & Masahide Kikkawa & Chikara Furusawa & Wataru Iwasaki, 2025.
"Repeatability of protein structural evolution following convergent gene fusions,"
Nature Communications, Nature, vol. 16(1), pages 1-14, December.
Handle:
RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-63898-x
DOI: 10.1038/s41467-025-63898-x
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