Properties of a DNA-binding protein from rat nuclear scaffold fraction.
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.
Hibino
Y
Y
Cell Biology Division, Faculty of Pharmaceutical Sciences, Toyama Medical & Pharmaceutical University, Japan.
Tsukada
S
S
Sugano
N
N
D000818:Animals; D001483:Base Sequence; D002503:Centromere; D004247:DNA / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000378:metabolism*; D015252:Deoxyribonucleases, Type II Site-Specific / Q000378:metabolism; D004214:Distamycins / Q000378:metabolism; D008969:Molecular Sequence Data; D015530:Nuclear Matrix / Q000737:chemistry*; D051381:Rats; D012091:Repetitive Sequences, Nucleic Acid; D015183:Restriction Mapping
D004268:DNA-Binding Proteins; D004214:Distamycins; C030000:stallimycin; D004247:DNA; C028649:endodeoxyribonuclease XmnI; D015252:Deoxyribonucleases, Type II Site-Specific; C027046:TCGA-specific type II deoxyribonucleases