title: Histones bind to contractile proteins and inhibit actomyosin ATPase.
abstract: Nuclear histones bind to and precipitate the major contractile proteins, actin and myosin. The binding of histone to actin seems to reach saturation at 2:1 ratio, the interaction may serve some regulatory function(s) in intranuclear events. The binding of histone to myosin is not saturable, and, although it inhibits the actin-activated Mg2+-dependent myosin ATPase activity, does therefore not seem of physiological importance.
authors.affiliation: Institut für Zoologie, Technische Hochschule, Darmstadt, FRG.
authors.forename: U
authors.initials: U
authors.lastname: Gröschel-Stewart
authors.forename: S
authors.initials: S
authors.lastname: Lehmann-Klose
authors.forename: E
authors.initials: E
authors.lastname: Magel
authors.forename: P
authors.initials: P
authors.lastname: Baumgart
mesh_terms: D000199:Actins / Q000032:analysis / Q000494:pharmacology; D000205:Actomyosin / Q000494:pharmacology; D000818:Animals; D001665:Binding Sites; D002645:Chickens; D003285:Contractile Proteins / Q000032:analysis*; D006657:Histones / Q000032:analysis* / Q000502:physiology; D009218:Myosins / Q000032:analysis / Q000037:antagonists & inhibitors*; D009391:Nephelometry and Turbidimetry; D014461:Ultracentrifugation
chemical_list: D000199:Actins; D003285:Contractile Proteins; D006657:Histones; D000205:Actomyosin; D009218:Myosins