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 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.

scholarly journals Possible role of histone acetylation and histone H1° replacement for the initiation of replication in regenerating rat liver

1991 ◽  
Vol 280 (3) ◽  
pp. 777-781
Author(s):  
G Weiss ◽  
H Talasz ◽  
B Puschendorf
Keyword(s):  
Dna Synthesis ◽  
Histone Acetylation ◽  
Rat Liver ◽  
Histone Acetyltransferase ◽  
Histone H1 ◽  
Acetyltransferase Activity ◽  
Initiation Of Replication ◽  
Histone Acetyltransferase Activity

The role of histone acetylation and DNA synthesis has been investigated extensively in the regenerating rat liver system in the presence and absence of the cyclophosphamide derivative mafosfamide. We demonstrate a mafosfamide-induced inhibition of maximum histone acetyltransferase activity followed by a second elevation of enzyme activity and an accompanying total suppression of DNA synthesis for 7-8 h. The maximum of histone acetyltransferase activity, in parallel with an elevated acetylation in vivo, the consecutive replacement of histone H1(0) amd initiation of replication occur sequentially in the presence and absence of mafosfamide, but with a temporary delay of 7-8 h. Our data indicate that modifications of histone acetyltransferase (EC 2.3.1.48) activity do not significantly influence the acetylation patterns of histones H3 and H4. The mafosfamide-induced change of histone acetyltransferase activity and acetylation in vivo, the shift of histone H1(0) exchange and the consecutive transition of initiation of replication suggest that these three events might be functionally related.

scholarly journals Histone acetyltransferase activity of yeast Gcn5p is required for the activation of target genes in vivo

1998 ◽  
Vol 12 (5) ◽  
pp. 627-639 ◽  
Author(s):  
M.-H. Kuo ◽  
J. Zhou ◽  
P. Jambeck ◽  
M. E.A. Churchill ◽  
C. D. Allis
Keyword(s):  
Target Genes ◽  
Histone Acetyltransferase ◽  
Acetyltransferase Activity ◽  
Histone Acetyltransferase Activity

scholarly journals Characterization of high molecular weight forms of peptide drugs in vivo.

1984 ◽  
Vol 7 (12) ◽  
pp. 917-922 ◽  
Author(s):  
KATSUHIKO OKUMURA ◽  
YOSHIHIRO SAITO ◽  
MASAO YASUHARA ◽  
RYOHEI HORI
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Peptide Drugs

Extraction and characterization of the enzymes of fructan biosynthesis in timothy (Phleum pratense)

1986 ◽  
Vol 64 (9) ◽  
pp. 1884-1887 ◽  
Author(s):  
Michio Suzuki ◽  
Christopher J. Pollock
Keyword(s):  
Molecular Weight ◽  
Higher Plants ◽  
Molecular Size ◽  
Phleum Pratense ◽  
Ph Optimum ◽  
Diethyl Dithiocarbamate ◽  
Phleum Pratense L ◽  
Sodium Diethyl Dithiocarbamate

A preparation of phlein sucrase from seedling shoots of timothy (Phleum pratense L.) is described which catalyzed the synthesis of fructan with a mean molecular size of 34 000 using sucrose as the substrate. Activity was fully sedimentable at 25 000 × g, had a pH optimum of 7.0, and a Km for sucrose of 0.15 M. Activity was inhibited by β-mercaptoethanol and sodium diethyl dithiocarbamate. Raffinose and stachyose, but not members of the kestose series of oligofructans, could act as fructosyl donors in addition to sucrose. Formation of oligosaccharides during high molecular weight fructan synthesis was minimal, with synthesis occurring by a mechanism apparently analogous to bacterial levansucrase. These observations are discussed in relation to the in vivo patterns of fructan biosynthesis observed in different species of higher plants.

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