{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Bobadilla Ugarte P"],"funding":["European Molecular Biology Organization","European Research Council","Dutch Research Council (NWO)","National Council on Science and Technology"],"pagination":["1920-1937.e10"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12094033"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["85(10)"],"pubmed_abstract":["Prokaryotic Argonaute proteins (pAgos) from the long-A clade are stand-alone immune systems that use small interfering DNA (siDNA) guides to recognize and cleave invading plasmid and virus DNA. Certain long-A pAgos are co-encoded with accessory proteins with unknown functions. Here, we show that cyanobacterial long-A pAgos act in conjunction with Argonaute-associated Cas4 family enzyme 1 (ACE1). Structural and biochemical analyses reveal that ACE1-associated pAgos mediate siDNA-guided DNA interference, akin to stand-alone pAgos. ACE1 is structurally homologous to the nuclease domain of bacterial DNA repair complexes and acts as a single-stranded DNA endonuclease that processes siDNA guides. pAgo and ACE1 form a heterodimeric long-A pAgo-ACE1 (APACE1) complex, which modulates ACE1 activity."],"journal":["Molecular cell"],"pubmed_title":["Cyanobacterial Argonautes and Cas4 family nucleases cooperate to interfere with invading DNA."],"pmcid":["PMC12094033"],"funding_grant_id":["016.Veni.192.072","948783"],"pubmed_authors":["Bobadilla Ugarte P","Hauryliuk V","Boeren S","Westphal AH","Mutte SK","Barendse P","Halter S","Heijstek C","Terenin I","Swarts DC","Jinek M","Niault T","Roosjen M","Koopal B"],"additional_accession":[]},"is_claimable":false,"name":"Cyanobacterial Argonautes and Cas4 family nucleases cooperate to interfere with invading DNA.","description":"Prokaryotic Argonaute proteins (pAgos) from the long-A clade are stand-alone immune systems that use small interfering DNA (siDNA) guides to recognize and cleave invading plasmid and virus DNA. Certain long-A pAgos are co-encoded with accessory proteins with unknown functions. Here, we show that cyanobacterial long-A pAgos act in conjunction with Argonaute-associated Cas4 family enzyme 1 (ACE1). Structural and biochemical analyses reveal that ACE1-associated pAgos mediate siDNA-guided DNA interference, akin to stand-alone pAgos. ACE1 is structurally homologous to the nuclease domain of bacterial DNA repair complexes and acts as a single-stranded DNA endonuclease that processes siDNA guides. pAgo and ACE1 form a heterodimeric long-A pAgo-ACE1 (APACE1) complex, which modulates ACE1 activity.","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 May","modification":"2026-06-01T10:22:16.588Z","creation":"2026-04-08T11:22:02.708Z"},"accession":"S-EPMC12094033","cross_references":{"pubmed":["40288374"],"doi":["10.1016/j.molcel.2025.03.025"]}}