{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zaremba M"],"funding":["Wellcome Trust"],"pagination":["13887-96"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4267653"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["42(22)"],"pubmed_abstract":["The stress-sensitive restriction-modification (RM) system CglI from Corynebacterium glutamicum and the homologous NgoAVII RM system from Neisseria gonorrhoeae FA1090 are composed of three genes: a DNA methyltransferase (M.CglI and M.NgoAVII), a putative restriction endonuclease (R.CglI and R.NgoAVII, or R-proteins) and a predicted DEAD-family helicase/ATPase (N.CglI and N.NgoAVII or N-proteins). Here we report a biochemical characterization of the R- and N-proteins. Size-exclusion chromatography and SAXS experiments reveal that the isolated R.CglI, R.NgoAVII and N.CglI proteins form homodimers, while N.NgoAVII is a monomer in solution. Moreover, the R.CglI and N.CglI proteins assemble in a complex with R2N2 stoichiometry. Next, we show that N-proteins have ATPase activity that is dependent"],"journal":["Nucleic acids research"],"pubmed_title":["DNA cleavage by CgII and NgoAVII requires interaction between N- and R-proteins and extensive nucleotide hydrolysis."],"pmcid":["PMC4267653"],"funding_grant_id":["084086"],"pubmed_authors":["Zaremba M","Szczelkun MD","Tamulaitiene G","Grigaitis R","Manakova E","Siksnys V","Silanskas A","Toliusis P"],"additional_accession":[]},"is_claimable":false,"name":"DNA cleavage by CgII and NgoAVII requires interaction between N- and R-proteins and extensive nucleotide hydrolysis.","description":"The stress-sensitive restriction-modification (RM) system CglI from Corynebacterium glutamicum and the homologous NgoAVII RM system from Neisseria gonorrhoeae FA1090 are composed of three genes: a DNA methyltransferase (M.CglI and M.NgoAVII), a putative restriction endonuclease (R.CglI and R.NgoAVII, or R-proteins) and a predicted DEAD-family helicase/ATPase (N.CglI and N.NgoAVII or N-proteins). Here we report a biochemical characterization of the R- and N-proteins. Size-exclusion chromatography and SAXS experiments reveal that the isolated R.CglI, R.NgoAVII and N.CglI proteins form homodimers, while N.NgoAVII is a monomer in solution. Moreover, the R.CglI and N.CglI proteins assemble in a complex with R2N2 stoichiometry. Next, we show that N-proteins have ATPase activity that is dependent","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014 Dec","modification":"2025-05-29T22:23:13.276Z","creation":"2025-05-29T22:23:13.276Z"},"accession":"S-EPMC4267653","cross_references":{"pubmed":["25429977"],"doi":["10.1093/nar/gku1236"]}}