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- W3129291247 abstract "Type III CRISPR-Cas systems initiate an intracellular signaling pathway to confer immunity. The signalling pathway includes synthesis of cyclic oligo-adenylate (cOA) and activation of the RNase activity of type III accessory ribonuclease Csm6/Csx1 by cOA. After immune response, cOA should be cleared on time to avoid constant cellular RNA degradation. In this study, we show that the majority of cOA degradation activity is metal-dependent and associated to cell membrane in Sulfolobus islandicus. Further, a membrane-associated DHH-DHHA1 family nuclease (MAD) rapidly cleaves cOA and deactivates Csx1 ribonuclease. Compared to cellular ring nuclease, MAD uses a metal-dependent hydrolysis mechanism and is much more active. However, the subcellular organization may prevent it degrade nascent cOA. Together, the data suggest that MAD act as the second cOA degrader after ring nuclease to remove diffused redundant cOA." @default.
- W3129291247 created "2021-03-01" @default.
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- W3129291247 date "2020-01-01" @default.
- W3129291247 modified "2023-09-23" @default.
- W3129291247 title "A Membrane-Associated Nuclease Degrades Cyclic Oligo-Adenylate and Deactivates Type III CRISPR Ribonuclease" @default.
- W3129291247 doi "https://doi.org/10.2139/ssrn.3551618" @default.
- W3129291247 hasPublicationYear "2020" @default.
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