{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Baudry K"],"funding":["Labex Saclay Plant Sciences-SPS","US National Science Foundation - Israel-US Binational Science Foundation","Agence Nationale de la Recherche","European Union","US National Science Foundation – Israel-US Binational Science Foundation"],"pagination":["gkag033"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12825314"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["54(3)"],"pubmed_abstract":["RNase J (RNJ) is a ribonuclease found in bacteria, archaea, and plant chloroplasts, and plays diverse roles in RNA maturation and stability. Chloroplast RNJ is encoded by the nuclear RNJ locus and is essential for embryo maturation. Arabidopsis or tobacco plants depleted for RNJ accumulate massive amounts of double-stranded RNA (dsRNA), which interferes with translation and causes chlorosis. Land plant RNJ uniquely contains a C-terminal GT1 domain, a DNA-binding motif found in transcription factors. Here, we have used complementation of an Arabidopsis rnj mutant with versions of RNJ with a mutated or deleted GT1 domain to investigate its role in RNJ function. We show that in vitro, the recombinant GT1 domain binds both dsRNA and DNA, but not single-stranded nucleic acids, with no sequence "],"journal":["Nucleic acids research"],"pubmed_title":["The GT1 domain of RNase J ensures RNA quality control through dsRNA binding in Arabidopsis plastids."],"pmcid":["PMC12825314"],"funding_grant_id":["ANR-17-EUR-0007","101087830","2019631","MCB-2005794","ANR-20-CE20-0004 JOAQUIN","2023288"],"pubmed_authors":["Launay-Avon A","Delannoy E","Kleifeld O","Burstein C","Baudry K","Liehrmann A","Stern DB","Schuster G","Ceminsky M","Liveanu V","Skiada S","Castandet B"],"additional_accession":[]},"is_claimable":false,"name":"The GT1 domain of RNase J ensures RNA quality control through dsRNA binding in Arabidopsis plastids.","description":"RNase J (RNJ) is a ribonuclease found in bacteria, archaea, and plant chloroplasts, and plays diverse roles in RNA maturation and stability. Chloroplast RNJ is encoded by the nuclear RNJ locus and is essential for embryo maturation. Arabidopsis or tobacco plants depleted for RNJ accumulate massive amounts of double-stranded RNA (dsRNA), which interferes with translation and causes chlorosis. Land plant RNJ uniquely contains a C-terminal GT1 domain, a DNA-binding motif found in transcription factors. Here, we have used complementation of an Arabidopsis rnj mutant with versions of RNJ with a mutated or deleted GT1 domain to investigate its role in RNJ function. We show that in vitro, the recombinant GT1 domain binds both dsRNA and DNA, but not single-stranded nucleic acids, with no sequence ","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Jan","modification":"2026-06-13T03:10:17.796Z","creation":"2026-06-13T03:08:39.794Z"},"accession":"S-EPMC12825314","cross_references":{"pubmed":["41569155"],"doi":["10.1093/nar/gkag033"]}}