Abstract
An ADP-ribosyltransferase from turkey erythrocytes which utilizes proteins and low molecular weight guanidino compounds such as arginine and agmatine as ADP-ribose acceptors was stimulated by histones. The effect was specific in that choleragen, a bacterial mono(ADP-ribosyl)transferase that increased adenylate cyclase activity in animal cells, was not activated by histones. With the erythrocyte enzyme, histones decreased the apparent Km values for arginine methyl ester and agmatine and increased the stability of the transferase to thermal denaturation. Activation of the transferase by histones was rapid, with a minimal delay observed upon addition of histones to a histone-free assay. Activation by histones was reversed upon dilution of a sample containing histones into an assay mix free of histone. In the absence of histone, the transferase existed as a rapidly sedimenting species; in the presence of histone, the transferase sedimented as a protomer.
Highlights
An ADP-ribosyltransferase from turkeryythrocytes which utilizes proteins and low molecularweight guanidinocompoundssuch as arginineandagmatine as ADP-ribose acceptors was stimulated byhistones
Activity of the erythrocyte ADP-ribosyltransferase assayed with subsaturating concentrationof ADP-ribose acceptor was markedly increased by histone
Histone produced an activation of the transferase using limiting concentrations of agmatine which wassimilar to that produced by 200 mM NaCl (Fig. 5)
Summary
Val. 257, No 4, h u e of February 25, pp. 1660-1663, 1982 Printed in U.S.A. From the +Laboratoryof Cellular Metabolism and the $Molecular DiseaseBranch, National HeartL, ung, a n d Blood Institute, National Institutesof Health, Bethesda, Maryland 20205. An ADP-ribosyltransferase from turkeryythrocytes which utilizes proteins and low molecularweight guanidinocompoundssuch as arginineandagmatine as ADP-ribose acceptors was stimulated byhistones. The independent forms of the transferase; activation by histones appears tobe rapid and reversible
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