期刊
MOLECULAR CELL
卷 77, 期 4, 页码 709-+出版社
CELL PRESS
DOI: 10.1016/j.molcel.2019.12.009
关键词
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资金
- University of California (UC) San Diego Quantitative and Integrative Biology training grant [NIH T32 GM127235]
- NIH [T32 HL007444, T32 GM007752, F31 CA236405, K01 DK116917, P30 DK063491, S10 OD020025, R01 ES027595, R01 GM129245]
- Ludwig Institute for Cancer Research
- University of California, San Diego
Bacteria are continually challenged by foreign invaders, including bacteriophages, and have evolved a variety of defenses against these invaders. Here, we describe the structural and biochemical mechanisms of a bacteriophage immunity pathway found in a broad array of bacteria, including E. coli and Pseudomonas aeruginosa. This pathway uses eukaryotic-like HORMA domain proteins that recognize specific peptides, then bind and activate a cGAS/DncV-like nucleotidyltransferase (CD-NTase) to generate a cyclic triadenylate (cAAA) second messenger; cAAA in turn activates an endonuclease effector, NucC. Signaling is attenuated by a homolog of the AAA+ ATPase Pch2/TRIP13, which binds and disassembles the active HORMA-CD-NTase complex. When expressed in non-pathogenic E. coli, this pathway confers immunity against bacteriophage lambda through an abortive infection mechanism. Our findings reveal the molecular mechanisms of a bacterial defense pathway integrating a cGAS-like nucleotidyltransferase with HORMA domain proteins for threat sensing through protein detection and negative regulation by a Trip13 ATPase.
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