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TitleMultiple enzymatic activities of a Sir2-HerA system cooperate for anti-phage defense.
Journal, issue, pagesMol Cell, Vol. 83, Issue 24, Page 4600-44613.e6, Year 2023
Publish dateDec 21, 2023
AuthorsDongmei Tang / Yijun Chen / Hao Chen / Tingting Jia / Qiang Chen / Yamei Yu /
PubMed AbstractIn response to the persistent exposure to phage infection, bacteria have evolved diverse antiviral defense mechanisms. In this study, we report a bacterial two-component defense system consisting of ...In response to the persistent exposure to phage infection, bacteria have evolved diverse antiviral defense mechanisms. In this study, we report a bacterial two-component defense system consisting of a Sir2 NADase and a HerA helicase. Cryo-electron microscopy reveals that Sir2 and HerA assemble into a ∼1 MDa supramolecular octadecamer. Unexpectedly, this complex exhibits various enzymatic activities, including ATPase, NADase, helicase, and nuclease, which work together in a sophisticated manner to fulfill the antiphage function. Therefore, we name this defense system "Nezha" after a divine warrior in Chinese mythology who employs multiple weapons to defeat enemies. Our findings demonstrate that Nezha could sense phage infections, self-activate to arrest cell growth, eliminate phage genomes, and subsequently deactivate to allow for cell recovery. Collectively, Nezha represents a paradigm of sophisticated and multifaceted strategies bacteria use to defend against viral infections.
External linksMol Cell / PubMed:38096825
MethodsEM (single particle)
Resolution2.97 Å
Structure data

35978

8j4u

EMDB-35978, PDB-8j4u:
Structure of HerA-Sir2 complex from Escherichia coli Nezha system
Method: EM (single particle) / Resolution: 2.97 Å

Chemicals

ChemComp-AR6:
[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL

ChemComp-AGS:
PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-gamma-S, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

Source
  • escherichia coli (E. coli)
KeywordsIMMUNE SYSTEM / defense system HerA Sir2

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