[Interaction of subunits of cAMP-dependent protein kinase with structural elements of the cell nucleus].
Using the method of protein transfer from polyacrylamide gel to nitrocellulose filters with subsequent incubation of filter-adsorbed protein with [32P]DNA, it was found that the catalytic subunit of cAMP-dependent protein kinase from porcine brain is capable of interacting with DNA to form a stable complex. This complex is resistant even to 2 M NaCl. The ability of the catalytic subunit to interact with DNA depends on the degree of enzyme nativity. The regulatory subunit of cAMP-dependent protein kinase does not bind to DNA both in the presence and absence of cAMP. The 125I-labeled regulatory subunit can interact with some chromatin proteins, in particular, with histone H1 and core histones. An essential role in this binding belongs to electrostatic and hydrophobic interactions.
D000818:Animals; D001921:Brain / Q000201:enzymology; D002384:Catalysis; D002467:Cell Nucleus / Q000378:metabolism; D002850:Chromatography, Gel; D004262:DNA Restriction Enzymes / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000378:metabolism; D015246:Deoxyribonuclease EcoRI; D004591:Electrophoresis, Polyacrylamide Gel; D006657:Histones / Q000378:metabolism*; D066298:In Vitro Techniques; D007700:Kinetics; D047428:Protein Kinase Inhibitors; D011494:Protein Kinases / Q000378:metabolism*; D013552:Swine
D004268:DNA-Binding Proteins; D006657:Histones; D047428:Protein Kinase Inhibitors; D011494:Protein Kinases; D004262:DNA Restriction Enzymes; D015246:Deoxyribonuclease EcoRI
Izuchenie vzaimodeĭstviia sub''edinits cAMP-zavisimoĭ proteinkinazy so strukturnymi élementami iadra.