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Cyclic ADP ribose isomers : production, chemical structures, and immune signaling
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(2022) Cyclic ADP ribose isomers : production, chemical structures, and immune signaling. Science, 377 (6614). 1510. doi:10.1126/science.adc8969 ISSN 0036-8075.
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Official URL: http://dx.doi.org/10.1126/science.adc8969
Abstract
Cyclic adenosine diphosphate (ADP)–ribose (cADPR) isomers are signaling molecules produced by bacterial and plant Toll/interleukin-1 receptor (TIR) domains via nicotinamide adenine dinucleotide (oxidized form) (NAD+) hydrolysis. We show that v-cADPR (2′cADPR) and v2-cADPR (3′cADPR) isomers are cyclized by O-glycosidic bond formation between the ribose moieties in ADPR. Structures of 2′cADPR-producing TIR domains reveal conformational changes that lead to an active assembly that resembles those of Toll-like receptor adaptor TIR domains. Mutagenesis reveals a conserved tryptophan that is essential for cyclization. We show that 3′cADPR is an activator of ThsA effector proteins from the bacterial antiphage defense system termed Thoeris and a suppressor of plant immunity when produced by the effector HopAM1. Collectively, our results reveal the molecular basis of cADPR isomer production and establish 3′cADPR in bacteria as an antiviral and plant immunity–suppressing signaling molecule.
| Item Type: | Journal Article | ||||||||||||||||||||||||||||||||||||
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| Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) |
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| Journal or Publication Title: | Science | ||||||||||||||||||||||||||||||||||||
| Publisher: | American Association for the Advancement of Science | ||||||||||||||||||||||||||||||||||||
| ISSN: | 0036-8075 | ||||||||||||||||||||||||||||||||||||
| Official Date: | 30 September 2022 | ||||||||||||||||||||||||||||||||||||
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| Volume: | 377 | ||||||||||||||||||||||||||||||||||||
| Number: | 6614 | ||||||||||||||||||||||||||||||||||||
| Number of Pages: | 11 | ||||||||||||||||||||||||||||||||||||
| Article Number: | 1510 | ||||||||||||||||||||||||||||||||||||
| DOI: | 10.1126/science.adc8969 | ||||||||||||||||||||||||||||||||||||
| Status: | Peer Reviewed | ||||||||||||||||||||||||||||||||||||
| Publication Status: | Published | ||||||||||||||||||||||||||||||||||||
| Access rights to Published version: | Restricted or Subscription Access | ||||||||||||||||||||||||||||||||||||
| RIOXX Funder/Project Grant: |
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