Molecular basis of Gabija anti-phage supramolecular assemblies

Xiao Yuan Yang, Zhangfei Shen, Jiale Xie, Jacelyn Greenwald, Ila Marathe, Qingpeng Lin, Wen Jun Xie, Vicki H. Wysocki, Tian Min Fu

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish
JournalNature Structural and Molecular Biology
DOIs
StateAccepted/In press - 2024

Fingerprint

Dive into the research topics of 'Molecular basis of Gabija anti-phage supramolecular assemblies'. Together they form a unique fingerprint.

Cite this