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• W1567429542 abstract "Using oligonucleotide affinity chromatography with DNase I footprinting as an assay we have looked for proteins that interact with sequence elements within the yeast origin of replication, autonomously replicating sequence 1 (ARS1). In this work we describe a protein that binds with high affinity to DNA but displays only moderate sequence specificity. It is eluted at 0.7 M salt from an ARS1 oligonucleotide column. Footprinting analysis on ARS1 at a high protein concentration revealed at least three sites of protection flanking element A and its repeats. Element A itself is rendered hypersensitive to DNase I digestion upon protein binding. This pattern is also observed for the H4 and HMR-E ARSs, suggesting that the protein alters the DNA conformation at element A and its repeats. The affinity-purified fraction is also capable of supercoiling a relaxed, covalently closed plasmid in the presence of topoisomerase. Highly purified preparations of the protein are enriched in an 18-kDa polypeptide which can be renatured from a denaturing gel and shown to bind ARS1 DNA. We have designated this protein DBF-A, DNA-binding factor A." @default.
• W1567429542 created "2016-06-24" @default.
• W1567429542 creator A5000378293 @default.
• W1567429542 creator A5012607908 @default.
• W1567429542 date "1992-01-01" @default.
• W1567429542 modified "2023-09-26" @default.
• W1567429542 title "Identification and purification of DBF-A, a double-stranded DNA-binding protein from Saccharomyces cerevisiae." @default.
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• W1567429542 doi "https://doi.org/10.1016/s0021-9258(18)45994-7" @default.
• W1567429542 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/1730709" @default.
• W1567429542 hasPublicationYear "1992" @default.
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