Calf liver nuclear N-acetyltransferases. Purification and properties of two enzymes with both spermidine acetyltransferase and histone acetyltransferase activities.
作者： P.R. Libby
DOI: 10.1016/S0021-9258(17)38293-5
关键词: Histone 、 Spermidine 、 Enzyme 、 Biology 、 Acetylation 、 Acetyltransferase 、 Biochemistry 、 Spermidine acetylation 、 Histone acetyltransferase activity 、 Molecular biology 、 Histone acetyltransferase
摘要: Calf liver contains two nuclear N-acetyltransferases which are separated by chromatography on hydroxylapatite. Both acetyltransferase A and B will transfer acetate from acetyl-CoA to either histone or spermidine. The same protein catalyzes the reaction with both substrates; this is shown a constant ratio of spermidine activity over 5,000-fold purification identical heat denaturation kinetics for each enzyme. Histone preferentially acetylated when acceptors present. enzymes acetylate polyamines (spermidine, spermine, diaminodipropylamine) diamines. Acetyltransferase acetylates histones in order: whole greater than H4 H2A H3 H2B H1; = H1. Michaelis constants 2 X 10(-4)M 9 10(-6)M acetyl-CoA. has molecular weight 150,000; 175,000. strongly inhibited p-chloromercuribenzoate weakly EDTA.
sci-hub.st 参考文章(21)
S. C. Bondy, Sidney Roberts, Beatrice S. Morelos, Histone-acetylating enzyme of brain Biochemical Journal. ,vol. 119, pp. 665- 672 ,(1970) , 10.1042/BJ1190665
Amparo Cano, Angel Pestaña, Regulation of histone acetyltransferase activity during the development of Artemia salina: Characterization of an inhibitor in nauplius larvae Developmental Biology. ,vol. 54, pp. 276- 287 ,(1976) , 10.1016/0012-1606(76)90305-5
Michael C. Scrutton, Merton F. Utter, Albert S. Mildvan, Pyruvate Carboxylase VI. THE PRESENCE OF TIGHTLY BOUND MANGANESE Journal of Biological Chemistry. ,vol. 241, pp. 3480- 3487 ,(1966) , 10.1016/S0021-9258(18)99858-3
Nikolaus Seiler, M.Jawad Al-Therib, Acetyl-CoA:1,4-diaminobutane N-acetyltransferase occurence in vertebrate organs and subcellular localization Biochimica et Biophysica Acta. ,vol. 354, pp. 206- 212 ,(1974) , 10.1016/0304-4165(74)90007-5
D. Gallwitz, I. Sures, Histone acetylation. Purification and properties of three histone-specific acetyltransferases from rat thymus nuclei☆ Biochimica et Biophysica Acta. ,vol. 263, pp. 315- 328 ,(1972) , 10.1016/0005-2795(72)90085-2
Julian Davies, Raoul Benveniste, Enzymatic acetylation of aminoglycoside antibiotics by Escherichia coli carrying an R factor. Biochemistry. ,vol. 10, pp. 1787- 1796 ,(1971) , 10.1021/BI00786A009
Dieter Gallwitz, Acetylation of histones by a kinase from rat liver nuclei Biochemical and Biophysical Research Communications. ,vol. 32, pp. 117- 121 ,(1968) , 10.1016/0006-291X(68)90355-0
Jim Blankenship, Thomas Walle, Acetylation of spermidine and spermine by rat liver and kidney chromatin. Archives of Biochemistry and Biophysics. ,vol. 179, pp. 235- 242 ,(1977) , 10.1016/0003-9861(77)90108-4
Nicholas E. Dixon, Carlo Gazzola, Robert L. Blakeley, Burt Zerner, Letter: Jack bean urease (EC 3.5.1.5). A metalloenzyme. A simple biological role for nickel? Journal of the American Chemical Society. ,vol. 97, pp. 4131- 4133 ,(1975) , 10.1021/JA00847A045
V. G. Allfrey, R. Faulkner, A. E. Mirsky, ACETYLATION AND METHYLATION OF HISTONES AND THEIR POSSIBLE ROLE IN THE REGULATION OF RNA SYNTHESIS Proceedings of the National Academy of Sciences. ,vol. 51, pp. 786- 794 ,(1964) , 10.1073/PNAS.51.5.786