{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Liang Q"],"funding":["National Institute of Allergy and Infectious Diseases","NIAID NIH HHS","National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["e4374"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9214754"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["31(7)"],"pubmed_abstract":["The widespread CBASS (cyclic oligonucleotide-based anti-phage signaling system) immune systems in bacteria protect their hosts from bacteriophage infection by triggering programmed cell death. CBASS systems all encode a cyclic oligonucleotide synthase related to eukaryotic cGAS but use diverse regulators and effector proteins including nucleases, phospholipases, and membrane-disrupting proteins to effect cell death. Cap18 is a predicted 3'-5' exonuclease associated with hundreds of CBASS systems, whose structure, biochemical activities, and biological roles remain unknown. Here we show that Cap18 is a DEDDh-family exonuclease related to the bacterial exonucleases RNase T and Orn and has nonspecific 3'-5' DNA exonuclease activity. Cap18 is commonly found in CBASS systems with associated Cap"],"journal":["Protein science : a publication of the Protein Society"],"pubmed_title":["Structure and activity of a bacterial defense-associated 3'-5' exonuclease."],"pmcid":["PMC9214754"],"funding_grant_id":["T32 GM008326","F31 GM137600","R21 AI148814","T32 GM127235","R35 GM144121"],"pubmed_authors":["Ye Q","Lau RK","Ur SN","Liang Q","Corbett KD","Richey ST"],"additional_accession":[]},"is_claimable":false,"name":"Structure and activity of a bacterial defense-associated 3'-5' exonuclease.","description":"The widespread CBASS (cyclic oligonucleotide-based anti-phage signaling system) immune systems in bacteria protect their hosts from bacteriophage infection by triggering programmed cell death. CBASS systems all encode a cyclic oligonucleotide synthase related to eukaryotic cGAS but use diverse regulators and effector proteins including nucleases, phospholipases, and membrane-disrupting proteins to effect cell death. Cap18 is a predicted 3'-5' exonuclease associated with hundreds of CBASS systems, whose structure, biochemical activities, and biological roles remain unknown. Here we show that Cap18 is a DEDDh-family exonuclease related to the bacterial exonucleases RNase T and Orn and has nonspecific 3'-5' DNA exonuclease activity. Cap18 is commonly found in CBASS systems with associated Cap","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Jul","modification":"2026-04-08T11:48:25.771Z","creation":"2024-10-16T15:23:06.929Z"},"accession":"S-EPMC9214754","cross_references":{"pubmed":["35762727"],"doi":["10.1002/pro.4374"]}}