Open AccessBacteriophage protein Gp46 is a cross-species inhibitor of nucleoid-associated HU proteins
Author(s) -
Peipei Zhang,
Xiaohui Zhao,
Yawen Wang,
Ke Du,
Wenwen Wang,
Jianfeng Yu,
Gang Chang,
Stephen Matthews,
Hongliang Wang,
Bing Liu
Publication year - 2022
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.2116278119
Subject(s) - nucleoid , biology , escherichia coli , bacillus subtilis , dna , bacteriophage , bacteria , bacillus anthracis , microbiology and biotechnology , biochemistry , genetics , gene
Significance Histone-like protein fromEscherichia coli strain U93 (HU) protein is the most abundant nucleoid-associated protein in bacteria, which plays a fundamental role in chromosomal compaction and organization. It is essential for most bacteria as well as Apicomplexans, thus an important target for the development of antimicrobial and antimalaria drugs. We report Gp46 as a phage protein HU inhibitor. It inhibits HU ofBacillus subtilis by occupying its DNA binding site, thus preventing chromosome segregation during cell division. As key residues for the interaction are highly conserved, Gp46 interacts with HUs of a broad range of pathogens, including many pathogenic bacteria and Apicomplexan parasites likePlasmodium falciparum. Thus, this cross-species property could benefit antibiotic and antimalaria drug development that targets HU.