NDLI: A single histone acetyltransferase from Tetrahymena macronuclei catalyzes deposition-related acetylation of free histones and transcription-related acetylation of nucleosomal histones.

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A single histone acetyltransferase from Tetrahymena macronuclei catalyzes deposition-related acetylation of free histones and transcription-related acetylation of nucleosomal histones.

Content Provider	Scilit
Author	Chicoine, L. G. Richman, R. Cook, R. G. Gorovsky, M. A. Allis, C. D.
Copyright Year	1987
Description	Journal: Journal of Cell Biology A salt-extracted histone acetyltransferase activity from Tetrahymena macronuclei acetylates mostly histone H3 and H4 when free histones are used as substrate. Free histone H4 is acetylated first at position 11 (monoacetylated) or positions 11 and 4 (diacetylated). This activity strongly resembles in vivo, deposition-related acetylation of newly synthesized histones. When acetylase-free mononucleosomes are used as substrate, all four core histones are acetylated by the same extract, and H4 is acetylated first at position 7 (monoacetylated) or positions 7 and 4 (diacetylated). In this respect, the activity of the extract is indistinguishable from postsynthetic, transcription-related histone acetylation that occurs in vivo or in isolated nuclei. Heat inactivation curves with both substrates are indistinguishable, and free histones compete with chromatin for limiting amounts of enzyme activity. These results argue strongly that two distinct, biologically important histone acetylations, one deposition related and one transcription related, are carried out by a single acetyltransferase.
Related Links	http://jcb.rupress.org/content/105/1/127.full.pdf
ISSN	00221295
DOI	10.1083/jcb.105.1.127
Journal	Journal of Cell Biology
Issue Number	1
Volume Number	105
Language	English
Publisher	Rockefeller University Press
Publisher Date	1987-07-01
Access Restriction	Open
Subject Keyword	Journal: Journal of Cell Biology Biochemistry and Molecular Biology Free Histones Deposition Related Acetylates Mostly Histone Related Acetylation Indistinguishable
Content Type	Text
Resource Type	Article
Subject	Physiology

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