Structural insights into the DNA topoisomerase II of the African swine fever virus

Jingyuan Cong, Yuhui Xin, Huiling Kang, Yunge Yang, Chenlong Wang, Dongming Zhao, Xuemei Li (), Zihe Rao () and Yutao Chen ()
Additional contact information
Jingyuan Cong: Chinese Academy of Sciences
Yuhui Xin: Chinese Academy of Sciences
Huiling Kang: Tsinghua University
Yunge Yang: Chinese Academy of Sciences
Chenlong Wang: Tsinghua University
Dongming Zhao: Chinese Academy of Agricultural Sciences
Xuemei Li: Chinese Academy of Sciences
Zihe Rao: Chinese Academy of Sciences
Yutao Chen: Chinese Academy of Sciences

Nature Communications, 2024, vol. 15, issue 1, 1-12

Abstract: Abstract Type II topoisomerases are ubiquitous enzymes that play a pivotal role in modulating the topological configuration of double-stranded DNA. These topoisomerases are required for DNA metabolism and have been extensively studied in both prokaryotic and eukaryotic organisms. However, our understanding of virus-encoded type II topoisomerases remains limited. One intriguing example is the African swine fever virus, which stands as the sole mammalian-infecting virus encoding a type II topoisomerase. In this work, we use several approaches including cryo-EM, X-ray crystallography, and biochemical assays to investigate the structure and function of the African swine fever virus type II topoisomerase, pP1192R. We determine the structures of pP1192R in different conformational states and confirm its enzymatic activity in vitro. Collectively, our results illustrate the basic mechanisms of viral type II topoisomerases, increasing our understanding of these enzymes and presenting a potential avenue for intervention strategies to mitigate the impact of the African swine fever virus.

Date: 2024
References: View references in EconPapers View complete reference list from CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/s41467-024-49047-w 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:15:y:2024:i:1:d:10.1038_s41467-024-49047-w

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

DOI: 10.1038/s41467-024-49047-w

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 ().