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- W2021170422 abstract "A human cDNA was cloned that encodes a DNA-binding protein (SATB1) that is expressed predominantly in thymus and binds selectively to the nuclear matrix/scaffold-associating DNAs (MARs/SARs). Missing nucleoside experiments showed that SATB1 selectively binds in a special AT-rich sequence context where one strand consists of mixed A's, T's, and C's, excluding G's (ATC sequences). When this feature is destroyed by mutation, SATB1 binding is greatly reduced even if the direct contact sequence remains intact. Conjunctional SATB1-binding sequences become stably unpaired in supercoiled DNA. Specific mutations that diminish the unwinding potential greatly reduce SATB1 binding. However, SATB1 does not bind single-stranded DNA. Chemical interference assays show that SATB1 binds along the minor groove with very little contact with the bases. This suggests that SATB1 recognizes the ATC sequence indirectly through the altered sugar-phosphate backbone structure present in the double-stranded DNA." @default.
- W2021170422 created "2016-06-24" @default.
- W2021170422 creator A5045820275 @default.
- W2021170422 creator A5062254944 @default.
- W2021170422 creator A5068873662 @default.
- W2021170422 creator A5085467911 @default.
- W2021170422 date "1992-08-21" @default.
- W2021170422 modified "2023-10-02" @default.
- W2021170422 title "A tissue-specific MAR/SAR DNA-binding protein with unusual binding site recognition" @default.
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- W2021170422 doi "https://doi.org/10.1016/0092-8674(92)90432-c" @default.
- W2021170422 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/1505028" @default.
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