PMID: 2497781Jun 1, 1989Paper

Histone-lysine methyltransferase activity from sea-urchin embryo nuclei. Changes in substrate specificity upon purification

Biochimica Et Biophysica Acta
F AnielloL Tosi

Abstract

The S-adenosylmethionine:histone-lysine methyltransferase (EC 2.1.1.43) enzyme activity, present in the chromatin of sea-urchin embryo nuclei, has been purified about 300-fold with 30% overall yield. The initial activity in the nucleus transfers methyl groups to the epsilon-amino group of lysines and acceptor proteins are chromatin-bound H3 and H4 histones. In contrast, the purified enzyme activity transfers methyl groups to the arginines and acceptor proteins are soluble H3 and H4 histones. The two changes in substrate specificity do not occur at the same time. The variation of acceptor protein from chromatin-bound to soluble histones occurs at the first step, upon nuclei sonication, when no protein fractionation has yet been performed. At that step, lysine is still the only methylated side-chain. The variation of the methylated amino acid from lysine to arginine occurs gradually with increasing enzyme purification. The enzyme activity has a molecular mass of about 200 kDa. Saturation curves for H3 and H4 histones, used as substrate either individually or in total histones, and for AdoMet show no substantial dependence on enzyme purification. Maximal activity for the enzyme, at all purification levels, occurs at about pH 8 for...Continue Reading

References

Nov 1, 1986·Proceedings of the National Academy of Sciences of the United States of America·S K KarathanasisS E Antonarakis
Nov 22, 1985·Biochimica Et Biophysica Acta·J A Duerre, D V Onisk
Oct 13, 1983·Biochimica Et Biophysica Acta·M BrannoL Tosi
Dec 1, 1962·The Journal of Cell Biology·R T HINEGARDNER
Mar 17, 2010·Proceedings of the National Academy of Sciences of the United States of America·Thorsten KahntJohn-Dylan Haynes
Jan 10, 2012·Annals of Oncology : Official Journal of the European Society for Medical Oncology·J-L LeeH Ahn

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