Bacterial Hachiman complex executes DNA cleavage for antiphage defense

Yongqing Cui, Zhikang Dai, Yufei Ouyang, Chunyang Fu, Yanjing Wang, Xueting Chen, Kaiyue Yang, Shuyue Zheng, Wenwen Wang, Pan Tao, Zeyuan Guan () and Tingting Zou ()
Additional contact information
Yongqing Cui: Huazhong Agricultural University
Zhikang Dai: Huazhong Agricultural University
Yufei Ouyang: Huazhong Agricultural University
Chunyang Fu: Huazhong Agricultural University
Yanjing Wang: Huazhong Agricultural University
Xueting Chen: Huazhong Agricultural University
Kaiyue Yang: Huazhong Agricultural University
Shuyue Zheng: Huazhong Agricultural University
Wenwen Wang: Huazhong Agricultural University
Pan Tao: Huazhong Agricultural University
Zeyuan Guan: Huazhong Agricultural University
Tingting Zou: Huazhong Agricultural University

Nature Communications, 2025, vol. 16, issue 1, 1-12

Abstract: Abstract Bacteria have developed a variety of immune systems to combat phage infections. The Hachiman system is a novel prokaryotic antiphage defense system comprising HamA and HamB proteins, which contains the DUF1837 and helicase domains, respectively. However, the defense mechanism remains only partially understood. Here, we present the cryo-electron microscopy (cryo-EM) structure of the Hachiman defense system featuring a fusion of Cap4 nuclease domain within HamA. Further structure analysis indicates that the DUF1837 domain on HamA resembles the PD-(D/E)XK nuclease but lacks active sites. Bioinformatics analysis reveals that catalytically inactive DUF1837 domains often recruit other functional domains to fulfill anti-phage defense. HamA interacts with HamB to form a heterodimer HamAB to mediate ATP hydrolysis and execute DNA cleavage, thus implementing antiphage defense. Our findings elucidate the structural basis of the Hachiman defense complex, highlighting the critical roles of the helicase and nuclease in prokaryotic immunity.

Date: 2025
References: View references in EconPapers View complete reference list from CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-025-57851-1 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-57851-1

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-025-57851-1

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().