scholarly journals Assays of nucleosome assembly and the inhibition of histone acetyltransferase activity. (11) Digestion of chromatin; and (12) Purification and characterization of DNA after digestion of chromatin

2007 ◽  
Author(s):  
Takahito Yamasaki ◽  
Takehide Murata ◽  
Chunyuan Jin ◽  
Kohsuke Kato ◽  
Michiya Noguchi ◽  
...  
Keyword(s):  
Histone Acetyltransferase ◽  
Nucleosome Assembly ◽  
Purification And Characterization ◽  
Acetyltransferase Activity ◽  
Histone Acetyltransferase Activity

scholarly journals The TFIIIC90 Subunit of TFIIIC Interacts with Multiple Components of the RNA Polymerase III Machinery and Contains a Histone-Specific Acetyltransferase Activity

1999 ◽  
Vol 19 (11) ◽  
pp. 7697-7704 ◽  
Author(s):  
Yng-Ju Hsieh ◽  
Tapas K. Kundu ◽  
Zhengxin Wang ◽  
Robert Kovelman ◽  
Robert G. Roeder
Keyword(s):  
Rna Polymerase ◽  
Histone Acetyltransferase ◽  
Rna Polymerase Iii ◽  
Acetyltransferase Activity ◽  
Multiple Components ◽  
Polymerase Iii ◽  
Bona Fide ◽  
Human Transcription Factor ◽  
Histone Acetyltransferase Activity

ABSTRACT Human transcription factor IIIC (hTFIIIC) is a multisubunit complex that directly recognizes promoter elements and recruits TFIIIB and RNA polymerase III. Here we describe the cDNA cloning and characterization of the 90-kDa subunit (hTFIIIC90) that is present within a DNA-binding subcomplex (TFIIIC2) of TFIIIC. hTFIIIC90 has no specific homology to any of the known yeast TFIIIC subunits. Immunodepletion and immunoprecipitation studies indicate that hTFIIIC90 is a bona fide subunit of TFIIIC2 and absolutely required for RNA polymerase III transcription. hTFIIIC90 shows interactions with the hTFIIIC220, hTFIIIC110, and hTFIIIC63 subunits of TFIIIC, the hTFIIIB90 subunit of TFIIIB, and the human RPC39 (hRPC39) and hRPC62 subunits of an initiation-specific subcomplex of RNA polymerase III. These interactions may facilitate both TFIIIB and RNA polymerase III recruitment to the preinitiation complex by TFIIIC. We show that hTFIIIC90 has an intrinsic histone acetyltransferase activity with a substrate specificity for histone H3.

Partial Characterization of a Histone Acetyltransferase from Trout Testis

1975 ◽  
Vol 53 (7) ◽  
pp. 796-803 ◽  
Author(s):  
E. P. M. Candido
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Histone Acetyltransferase ◽  
Ph Optimum ◽  
Acetyltransferase Activity ◽  
Nuclear Extracts ◽  
Specific Activities ◽  
Histone Acetyltransferase Activity

Histone acetyltransferase activity of trout testis was studied both in intact nuclei, and in high salt nuclear extracts, With intact nuclei, the distribution of incorporated [14C]acetate in the various histones was similar to that observed in vivo; the arginine-rich histones H3 and H4 showed the highest specific activities, and lower amounts of label were detected in histones H2a and H2b. Histone H1 incorporated little or no label. Acetyltransferase activity could be detected in purified, sheared chromatin after the addition of MgCl2 or KCl, suggesting that the enzyme is bound to chromatin.Treatment of nuclei with 0,4 M NaCl caused the dissociation of acetyltransferase activity. Most of this solubilized activity failed to bind to DEAE Sephadex and behaved as a high molecular weight heterogeneous complex on Sephadex G-100, suggesting that the enzyme is present as an aggregate with other proteins in the extract. The pH optimum of this preparation was approximately 8.5, and the enzyme showed a preference for histones H3 and H4 as substrates.

scholarly journals Assays of nucleosome assembly and the inhibition of histone acetyltransferase activity

2007 ◽  
Author(s):  
Takahito Yamasaki ◽  
Takehide Murata ◽  
Chunyuan Jin ◽  
Kohsuke Kato ◽  
Michiya Noguchi ◽  
...  
Keyword(s):  
Histone Acetyltransferase ◽  
Nucleosome Assembly ◽  
Acetyltransferase Activity ◽  
Histone Acetyltransferase Activity
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