TY - JOUR
T1 - Molecular basis of Gabija anti-phage supramolecular assemblies
AU - Yang, Xiao Yuan
AU - Shen, Zhangfei
AU - Xie, Jiale
AU - Greenwald, Jacelyn
AU - Marathe, Ila
AU - Lin, Qingpeng
AU - Xie, Wen Jun
AU - Wysocki, Vicki H.
AU - Fu, Tian Min
N1 - Publisher Copyright:
© The Author(s), under exclusive licence to Springer Nature America, Inc. 2024.
PY - 2024
Y1 - 2024
N2 - As one of the most prevalent anti-phage defense systems in prokaryotes, Gabija consists of a Gabija protein A (GajA) and a Gabija protein B (GajB). The assembly and function of the Gabija system remain unclear. Here we present cryo-EM structures of Bacillus cereus GajA and GajAB complex, revealing tetrameric and octameric assemblies, respectively. In the center of the complex, GajA assembles into a tetramer, which recruits two sets of GajB dimer at opposite sides of the complex, resulting in a 4:4 GajAB supramolecular complex for anti-phage defense. Further biochemical analysis showed that GajA alone is sufficient to cut double-stranded DNA and plasmid DNA, which can be inhibited by ATP. Unexpectedly, the GajAB displays enhanced activity for plasmid DNA, suggesting a role of substrate selection by GajB. Together, our study defines a framework for understanding anti-phage immune defense by the GajAB complex.
AB - As one of the most prevalent anti-phage defense systems in prokaryotes, Gabija consists of a Gabija protein A (GajA) and a Gabija protein B (GajB). The assembly and function of the Gabija system remain unclear. Here we present cryo-EM structures of Bacillus cereus GajA and GajAB complex, revealing tetrameric and octameric assemblies, respectively. In the center of the complex, GajA assembles into a tetramer, which recruits two sets of GajB dimer at opposite sides of the complex, resulting in a 4:4 GajAB supramolecular complex for anti-phage defense. Further biochemical analysis showed that GajA alone is sufficient to cut double-stranded DNA and plasmid DNA, which can be inhibited by ATP. Unexpectedly, the GajAB displays enhanced activity for plasmid DNA, suggesting a role of substrate selection by GajB. Together, our study defines a framework for understanding anti-phage immune defense by the GajAB complex.
UR - http://www.scopus.com/inward/record.url?scp=85190641224&partnerID=8YFLogxK
U2 - 10.1038/s41594-024-01283-w
DO - 10.1038/s41594-024-01283-w
M3 - Article
AN - SCOPUS:85190641224
SN - 1545-9993
JO - Nature Structural and Molecular Biology
JF - Nature Structural and Molecular Biology
ER -