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 Human TFIIIC Relieves Chromatin-Mediated Repression of RNA Polymerase III Transcription and Contains an Intrinsic Histone Acetyltransferase Activity

1999 ◽  
Vol 19 (2) ◽  
pp. 1605-1615 ◽  
Author(s):  
Tapas K. Kundu ◽  
Zhengxin Wang ◽  
Robert G. Roeder
Keyword(s):  
Rna Polymerase ◽  
Histone Acetyltransferase ◽  
Rna Polymerase Iii ◽  
Acetyltransferase Activity ◽  
Naked Dna ◽  
Polymerase Iii ◽  
Chromatin Template ◽  
Direct Recognition ◽  
Histone Acetyltransferase Activity

ABSTRACT Human TFIIIC is a multisubunit factor that is essential for transcription by RNA polymerase III on tRNA and virus-associated RNA genes and initiates preinitiation complex assembly by direct recognition of promoter elements. We show that highly purified TFIIIC, at concentrations above those sufficient for transcription of naked DNA templates, effectively relieves nucleosome-mediated repression on an in vitro-reconstituted chromatin template. Highly purified TFIIIC alone can bind to the A and B boxes of a tRNA gene within a chromatin template and, further, displays a histone acetyltransferase activity that is intrinsic to at least one (and probably three) of its subunits. The possibility of a direct link between TFIIIC-dependent chromatin transcription and acetyltransferase activities is suggested by the partial loss of these activities, but not DNA transcription activity, following pretreatment of TFIIIC withp-hydroxymercuribenzoic acid.

Characterization of the U3 and U6 snRNA genes from wheat: U3 snRNA genes in monocot plants are transcribed by RNa polymerase III

1992 ◽  
Vol 19 (6) ◽  
pp. 973-983 ◽  
Author(s):  
Christopher Marshallsay ◽  
Sheila Connelly ◽  
Witold Filipowicz
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Iii ◽  
U6 Snrna ◽  
Polymerase Iii

scholarly journals Cloning and Characterization of Two Evolutionarily Conserved Subunits (TFIIIC102 and TFIIIC63) of Human TFIIIC and Their Involvement in Functional Interactions with TFIIIB and RNA Polymerase III

1999 ◽  
Vol 19 (7) ◽  
pp. 4944-4952 ◽  
Author(s):  
Yng-Ju Hsieh ◽  
Zhengxin Wang ◽  
Robert Kovelman ◽  
Robert G. Roeder
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Iii ◽  
Structure And Function ◽  
Class Iii ◽  
Tetratricopeptide Repeats ◽  
Helix Loop Helix ◽  
Polymerase Iii ◽  
And Function

ABSTRACT Human transcription factor IIIC (hTFIIIC) is a multisubunit complex that mediates transcription of class III genes through direct recognition of promoters (for tRNA and virus-associated RNA genes) or promoter-TFIIIA complexes (for the 5S RNA gene) and subsequent recruitment of TFIIIB and RNA polymerase III. We describe the cognate cDNA cloning and characterization of two subunits (hTFIIIC63 and hTFIIIC102) that are present within a DNA-binding subcomplex (TFIIIC2) of TFIIIC and are related in structure and function to two yeast TFIIIC subunits (yTFIIIC95 and yTFIIIC131) previously shown to interact, respectively, with the promoter (A box) and with a subunit of yeast TFIIIB. hTFIIIC63 and hTFIIIC102 show parallel in vitro interactions with the homologous human TFIIIB and RNA polymerase III components, as well as additional interactions that may facilitate both TFIIIB and RNA polymerase III recruitment. These include novel interactions of hTFIIIC63 with hTFIIIC102, with hTFIIIB90, and with hRPC62, in addition to the hTFIIIC102–hTFIIIB90 and hTFIIIB90–hRPC39 interactions that parallel the previously described interactions in yeast. As reported for yTFIIIC131, hTFIIIC102 contains acidic and basic regions, tetratricopeptide repeats (TPRs), and a helix-loop-helix domain, and mutagenesis studies have implicated the TPRs in interactions both with hTFIIIC63 and with hTFIIIB90. These observations further document conservation from yeast to human of the structure and function of the RNA polymerase III transcription machinery, but in addition, they provide new insights into the function of hTFIIIC and suggest direct involvement in recruitment of both TFIIIB and RNA polymerase III.

Characterization of the gene encoding the largest subunit of Plasmodium falciparum RNA polymerase III

1991 ◽  
Vol 46 (2) ◽  
pp. 229-239 ◽  
Author(s):  
Wu-Bo Li ◽  
David J. Bzik ◽  
Manami Tanaka ◽  
Haoming Gu ◽  
Barbara A. Fox ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Rna Polymerase ◽  
Rna Polymerase Iii ◽  
Gene Encoding ◽  
Polymerase Iii

Functional Characterization of Novel U6 RNA Polymerase III Promoters: Their Implication for CRISPR-Cas9-Mediated Gene Editing in Aspergillus oryzae

2019 ◽  
Vol 76 (12) ◽  
pp. 1443-1451 ◽  
Author(s):  
Chanikul Chutrakul ◽  
Sarocha Panchanawaporn ◽  
Sukanya Jeennor ◽  
Jutamas Anantayanon ◽  
Tayvich Vorapreeda ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Aspergillus Oryzae ◽  
Gene Editing ◽  
Functional Characterization ◽  
Rna Polymerase Iii ◽  
Polymerase Iii ◽  
U6 Rna

scholarly journals Characterization of new RNA polymerase III and RNA polymerase II transcriptional promoters in the Bovine Leukemia Virus genome

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Benoit Van Driessche ◽  
Anthony Rodari ◽  
Nadège Delacourt ◽  
Sylvain Fauquenoy ◽  
Caroline Vanhulle ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Bovine Leukemia Virus ◽  
Leukemia Virus ◽  
Rna Polymerase Iii ◽  
Virus Genome ◽  
Polymerase Iii ◽  
Transcriptional Promoters

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.

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