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Biochem Genet
1991 Feb 01;291-2:13-28. doi: 10.1007/bf00578236.
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Regulation of nuclear histone acetyltransferase by nucleic acids, histone.DNA complex, and chromatin.
Wong LJ
,
Sharpe DJ
.
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Nuclear histone acetyltransferase is found to be inhibited by various nucleic acids and components. Of the adenosine phosphates, the order of inhibitory potency is ATP greater than ADP greater than AMP. Among the nucleoside triphosphates, GTP seems to be the best inhibitor, followed by ATP, CTP, and UTP. Deoxymononucleotides have the same order of inhibition potential as their ribonucleotide counterparts, with inhibition constants in the low millimolar range. Oligonucleotides and polynucleotides are much better inhibitors than mononucleotides. The inhibition constants of the DNA molecules are size dependent. Molecules larger than 40 base pairs have inhibition constants less than 18 micrograms/ml, whereas molecules with decreasing numbers of base pairs have increasing magnitudes of inhibition constants. However, acetyltransferase has a lower affinity for free DNA molecules than for DNA.histone complexes as revealed by its interaction with DNA-Sepharose and histone.DNA-Sepharose columns. Furthermore, native chromatin depleted of endogenous histone acetyltransferase activity shows no inhibitory effect on the enzyme. Yet heated chromatin not only loses substrate activity but also becomes an inhibitor for the enzyme. Since unmodified sea urchin sperm chromatin has been shown to be a potent acetyltransferase inhibitor, it seems possible that DNA.histone complexes may be the true inhibitory species and that the conformational states of such complexes may serve as a regulatory mechanism in the control of the enzyme activity.
ALLFREY,
ACETYLATION AND METHYLATION OF HISTONES AND THEIR POSSIBLE ROLE IN THE REGULATION OF RNA SYNTHESIS.
1964, Pubmed
ALLFREY,
ACETYLATION AND METHYLATION OF HISTONES AND THEIR POSSIBLE ROLE IN THE REGULATION OF RNA SYNTHESIS.
1964,
Pubmed
Allegra,
Affinity chromatographic purification of nucleosomes containing transcriptionally active DNA sequences.
1987,
Pubmed
Belikoff,
Extensive purification of histone acetylase A, the major histone N-acetyl transferase activity detected in mammalian cell nuclei.
1980,
Pubmed
Cousens,
Different accessibilities in chromatin to histone acetylase.
1979,
Pubmed
Csordas,
On the biological role of histone acetylation.
1990,
Pubmed
Davie,
Acetylated histone H4 is preferentially associated with template-active chromatin.
1978,
Pubmed
Easton,
High-resolution electrophoretic analysis of the histones from embryos and sperm of Arbacia punctulata.
1972,
Pubmed
,
Echinobase
Felsenfeld,
Chromatin.
1978,
Pubmed
Fukushima,
Nucleosome-histone acetyltransferase from rat liver chromatin.
1980,
Pubmed
Garcea,
Comparative studies of histone acetylation in nucleosomes, nuclei, and intact cells. Evidence for special factors which modify acetylase action.
1980,
Pubmed
Hebbes,
A direct link between core histone acetylation and transcriptionally active chromatin.
1988,
Pubmed
Igo-Kemenes,
Chromatin.
1982,
Pubmed
Jackson,
Studies on highly metabolically active acetylation and phosphorylation of histones.
1975,
Pubmed
Kelner,
Porcine liver nuclear histone acetyltransferase. Partial purification and basic properties.
1984,
Pubmed
Kornberg,
Structure of chromatin.
1977,
Pubmed
Marzluff,
Transcription of ribonucleic acid in isolated mouse myeloma nuclei.
1973,
Pubmed
Palter,
The use of DNA-cellulose for analyzing histone-DNA interactions. Discovery of nucleosome-like histone binding to single-stranded DNA.
1979,
Pubmed
Simpson,
Structure of chromatin containing extensively acetylated H3 and H4.
1978,
Pubmed
Vidali,
Butyrate suppression of histone deacetylation leads to accumulation of multiacetylated forms of histones H3 and H4 and increased DNase I sensitivity of the associated DNA sequences.
1978,
Pubmed
Wong,
Kinetic mechanism of the reaction catalyzed by nuclear histone acetyltransferase from calf thymus.
1983,
Pubmed
Wong,
Effect of sea urchin sperm chromatin on histone acetylation.
1980,
Pubmed
,
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