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- W2057500898 abstract "Our previous work [Hibino et al. (1992) Biochem. Biophys. Res. Commun. 184, 853-858] has shown that a highly repetitive component in rat nuclear DNA forms a sequence-directed bend to have the binding affinity for the nuclear scaffold protein, P130. In the present experiment, the mobility shift DNA-binding assay suggested that the formation of the repetitive component-P130 complex is based on some cooperative mode of interaction. The DNase I footprint analysis revealed that the major binding region of this protein in the DNA is located near the center of the 370-bp XmnI repeat which has a strongly bent overall structure. These results imply that a nuclear scaffold protein such as P130 binds to sequence-directed bend(s) in a highly repetitive DNA to play an important role in construction of a higher-order chromatin structure." @default.
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- W2057500898 date "1993-11-01" @default.
- W2057500898 modified "2023-10-17" @default.
- W2057500898 title "Properties of a DNA-Binding Protein from Rat Nuclear Scaffold Fraction" @default.
- W2057500898 doi "https://doi.org/10.1006/bbrc.1993.2480" @default.
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