{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Keatch SA"],"funding":["Wellcome Trust","Biotechnology and Biological Sciences Research Council"],"pagination":["6540-6"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC1289078"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["33(20)"],"pubmed_abstract":["The nucleoid-associated protein, StpA, of Escherichia coli binds non-specifically to double-stranded DNA (dsDNA) and apparently forms bridges between adjacent segments of the DNA. Such a coating of protein on the DNA would be expected to hinder the action of nucleases. We demonstrate that StpA binding hinders dsDNA cleavage by both the non-specific endonuclease, DNase I, and by the site-specific type I restriction endonuclease, EcoKI. It requires approximately one StpA molecule per 250-300 bp of supercoiled DNA and approximately one StpA molecule per 60-100 bp on linear DNA for strong inhibition of the nucleases. These results support the role of StpA as a nucleoid-structuring protein which binds DNA segments together. The inhibition of EcoKI, which cleaves DNA at a site remote from its in"],"journal":["Nucleic acids research"],"pubmed_title":["StpA protein from Escherichia coli condenses supercoiled DNA in preference to linear DNA and protects it from digestion by DNase I and EcoKI."],"pmcid":["PMC1289078"],"funding_grant_id":["C17860"],"pubmed_authors":["Dryden DT","Keatch SA","Ladbury JE","Leonard PG"],"additional_accession":[]},"is_claimable":false,"name":"StpA protein from Escherichia coli condenses supercoiled DNA in preference to linear DNA and protects it from digestion by DNase I and EcoKI.","description":"The nucleoid-associated protein, StpA, of Escherichia coli binds non-specifically to double-stranded DNA (dsDNA) and apparently forms bridges between adjacent segments of the DNA. Such a coating of protein on the DNA would be expected to hinder the action of nucleases. We demonstrate that StpA binding hinders dsDNA cleavage by both the non-specific endonuclease, DNase I, and by the site-specific type I restriction endonuclease, EcoKI. It requires approximately one StpA molecule per 250-300 bp of supercoiled DNA and approximately one StpA molecule per 60-100 bp on linear DNA for strong inhibition of the nucleases. These results support the role of StpA as a nucleoid-structuring protein which binds DNA segments together. The inhibition of EcoKI, which cleaves DNA at a site remote from its in","dates":{"release":"2005-01-01T00:00:00Z","publication":"2005","modification":"2025-04-04T08:48:18.251Z","creation":"2019-03-27T01:25:31Z"},"accession":"S-EPMC1289078","cross_references":{"pubmed":["16299353"],"doi":["10.1093/nar/gki951"]}}