Hierarchy of binding sites for chromosomal proteins HMG 1 and 2 in supercoiled deoxyribonucleic acid.
The interaction of chromosomal proteins HMG 1 and 2 with various DNA structures has been examined with plasmid pPst-0.9, which contains DNA sequences that can form the Z-DNA conformation and palindromic sequences that can form cruciform structures. Direct binding and competition experiments with 32P-labeled plasmid indicated that proteins HMG 1 and 2 preferentially bind to supercoiled form I DNA as compared to double-stranded linear DNA. The preferential binding to form I is due to the presence of single-stranded regions in this DNA. The binding of HMG 1 and 2 to the form I plasmid results in inhibition of S1 nuclease digestion in a selective manner. The B-Z junction is preferentially protected as compared to the cruciform, which in turn is more protected than other minor S1-sensitive structures present in pPst-0.9. Our results indicate that the binding of HMG 1 and 2 proteins to DNA is not random in that HMG 1 and 2 can distinguish between various S1 nuclease sensitive sites in the plasmid. The existence of a hierarchy of DNA binding sites for these proteins suggests that they can selectively affect the structure of distinct regions in the genome.
Hamada
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Bustin
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D000199:Actins / Q000235:genetics; D001665:Binding Sites; D004262:DNA Restriction Enzymes / Q000378:metabolism; D004278:DNA, Superhelical / Q000378:metabolism*; D015246:Deoxyribonuclease EcoRI; D004587:Electrophoresis, Agar Gel; D004720:Endonucleases / Q000378:metabolism; D005374:Filtration; D006609:High Mobility Group Proteins / Q000378:metabolism*; D006801:Humans; D010957:Plasmids; D015719:Single-Strand Specific DNA and RNA Endonucleases
D000199:Actins; D004278:DNA, Superhelical; D006609:High Mobility Group Proteins; D004720:Endonucleases; D004262:DNA Restriction Enzymes; D015246:Deoxyribonuclease EcoRI; D015719:Single-Strand Specific DNA and RNA Endonucleases