Histone deacetylase. Association with a nuclease resistant, high molecular weight fraction of HeLa cell chromatin.

作者: C W Hay , E P Candido

DOI: 10.1016/S0021-9258(18)32725-X

关键词:

摘要: The chromatin-bound histone deacetylase of HeLa cells has been studied using endogenous [3H]acetyl-labeled polynucleosomes containing the enzyme, prepared in presence 40 mM butyrate. Histone was assayed upon removal butyrate, and it found that active enzyme is only association with a high molecular weight complex. This deacetylase-containing complex relatively resistant to digestion micrococcal nuclease. No activity on mononucleosomes or oligonucleosomes. Up 90% labeled acetyl groups are removed from complexes incubated absence Free histones poor substrate under these conditions, but deacetylated when they remains bound this 1-2 M NaCl does not dissociate during its reaction acetylated core histones. Under typical nuclease contains DNA size distribution 5-11 kilobase pairs variety nonhistone proteins. Comparison protein composition nuclear matrix preparations shows some similarities. Taken together, results chromatographic behavior, fragment sizes, suggest protein-protein interactions may be important maintaining structure also binding itself

参考文章(45)
L.S. Cousens, D. Gallwitz, B.M. Alberts, Different accessibilities in chromatin to histone acetylase. Journal of Biological Chemistry. ,vol. 254, pp. 1716- 1723 ,(1979) , 10.1016/S0021-9258(17)37831-6
A.W. Senear, R.D. Palmiter, Multiple structural features are responsible for the nuclease sensitivity of the active ovalbumin gene. Journal of Biological Chemistry. ,vol. 256, pp. 1191- 1198 ,(1981) , 10.1016/S0021-9258(19)69948-5
V Jackson, A Shires, R Chalkley, D K Granner, Studies on highly metabolically active acetylation and phosphorylation of histones. Journal of Biological Chemistry. ,vol. 250, pp. 4856- 4863 ,(1975) , 10.1016/S0021-9258(19)41247-7
T. Hutcheon, G.H. Dixon, B. Levy-Wilson, Transcriptionally active mononucleosomes from trout testis are heterogeneous in composition. Journal of Biological Chemistry. ,vol. 255, pp. 681- 685 ,(1980) , 10.1016/S0021-9258(19)86231-2
J. Covault, R. Chalkley, The identification of distinct populations of acetylated histone. Journal of Biological Chemistry. ,vol. 255, pp. 9110- 9116 ,(1980) , 10.1016/S0021-9258(19)70534-1
Giorgio Vidali, Lidia C. Boffa, Vincent G. Allfrey, Properties of an Acidic Histone-binding Protein Fraction from Cell Nuclei Journal of Biological Chemistry. ,vol. 247, pp. 7365- 7373 ,(1972) , 10.1016/S0021-9258(19)44638-3
Linda Sealy, Roger Chalkley, The effect of sodium butyrate on histone modification Cell. ,vol. 14, pp. 115- 121 ,(1978) , 10.1016/0092-8674(78)90306-9