scholarly journals TATA box-binding protein (TBP) is a constituent of the polymerase I-specific transcription initiation factor TIF-IB (SL1) bound to the rRNA promoter and shows differential sensitivity to TBP-directed reagents in polymerase I, II, and III transcription factors.

1994 ◽  
Vol 14 (1) ◽  
pp. 597-605 ◽  
Author(s):  
C A Radebaugh ◽  
J L Matthews ◽  
G K Geiss ◽  
F Liu ◽  
J M Wong ◽  
...  
Keyword(s):  
Transcription Initiation ◽  
Binding Protein ◽  
Acanthamoeba Castellanii ◽  
Differential Sensitivity ◽  
Initiation Factor ◽  
Transcription Initiation Factor ◽  
I Factor ◽  
Tata Box Binding Protein ◽  
Polymerase I

The role of the Acanthamoeba castellanii TATA-binding protein (TBP) in transcription was examined. Specific antibodies against the nonconserved N-terminal domain of TBP were used to verify the presence of TBP in the fundamental transcription initiation factor for RNA polymerase I, TIF-IB, and to demonstrate that TBP is part of the committed initiation complex on the rRNA promoter. The same antibodies inhibit transcription in all three polymerase systems, but they do so differentially. Oligonucleotide competitors were used to evaluate the accessibility of the TATA-binding site in TIF-IB, TFIID, and TFIIIB. The results suggest that insertion of TBP into the polymerase II and III factors is more similar than insertion into the polymerase I factor.

TATA box-binding protein (TBP) is a constituent of the polymerase I-specific transcription initiation factor TIF-IB (SL1) bound to the rRNA promoter and shows differential sensitivity to TBP-directed reagents in polymerase I, II, and III transcription factors

1994 ◽  
Vol 14 (1) ◽  
pp. 597-605
Author(s):  
C A Radebaugh ◽  
J L Matthews ◽  
G K Geiss ◽  
F Liu ◽  
J M Wong ◽  
...  
Keyword(s):  
Transcription Initiation ◽  
Binding Protein ◽  
Acanthamoeba Castellanii ◽  
Differential Sensitivity ◽  
Initiation Factor ◽  
Transcription Initiation Factor ◽  
I Factor ◽  
Tata Box Binding Protein ◽  
Polymerase I

The role of the Acanthamoeba castellanii TATA-binding protein (TBP) in transcription was examined. Specific antibodies against the nonconserved N-terminal domain of TBP were used to verify the presence of TBP in the fundamental transcription initiation factor for RNA polymerase I, TIF-IB, and to demonstrate that TBP is part of the committed initiation complex on the rRNA promoter. The same antibodies inhibit transcription in all three polymerase systems, but they do so differentially. Oligonucleotide competitors were used to evaluate the accessibility of the TATA-binding site in TIF-IB, TFIID, and TFIIIB. The results suggest that insertion of TBP into the polymerase II and III factors is more similar than insertion into the polymerase I factor.

scholarly journals Effects of single-base substitutions within the Acanthamoeba castellanii rRNA promoter on transcription and on binding of transcription initiation factor and RNA polymerase I.

1988 ◽  
Vol 8 (2) ◽  
pp. 747-753 ◽  
Author(s):  
P Kownin ◽  
E Bateman ◽  
M R Paule
Keyword(s):  
Transcription Initiation ◽  
Single Point ◽  
Point Mutations ◽  
Acanthamoeba Castellanii ◽  
Dnase I ◽  
Initiation Factor ◽  
Rrna Gene ◽  
Transcription Initiation Factor ◽  
Polymerase I

Single-point mutations were introduced into the promoter region of the Acanthamoeba castellanii rRNA gene by chemical mutagen treatment of a single-stranded clone in vitro, followed by reverse transcription and cloning of the altered fragment. The promoter mutants were tested for transcription initiation factor (TIF) binding by a template commitment assay plus DNase I footprinting and for transcription by an in vitro runoff assay. Point mutations within the previously identified TIF interaction region (between -20 and -47, motifs A and B) indicated that TIF interacts most strongly with a sequence centered at -29 and less tightly with sequences upstream and downstream. Some alterations of the base sequence closer to the transcription start site (and outside the TIF-protected site) also significantly decreased specific RNA synthesis in vitro. These were within the region which is protected from DNase I digestion by polymerase I, but these mutations did not detectably affect the binding of polymerase to the promoter.

Effects of single-base substitutions within the Acanthamoeba castellanii rRNA promoter on transcription and on binding of transcription initiation factor and RNA polymerase I

1988 ◽  
Vol 8 (2) ◽  
pp. 747-753
Author(s):  
P Kownin ◽  
E Bateman ◽  
M R Paule
Keyword(s):  
Transcription Initiation ◽  
Single Point ◽  
Point Mutations ◽  
Acanthamoeba Castellanii ◽  
Dnase I ◽  
Initiation Factor ◽  
Rrna Gene ◽  
Transcription Initiation Factor ◽  
Polymerase I

Single-point mutations were introduced into the promoter region of the Acanthamoeba castellanii rRNA gene by chemical mutagen treatment of a single-stranded clone in vitro, followed by reverse transcription and cloning of the altered fragment. The promoter mutants were tested for transcription initiation factor (TIF) binding by a template commitment assay plus DNase I footprinting and for transcription by an in vitro runoff assay. Point mutations within the previously identified TIF interaction region (between -20 and -47, motifs A and B) indicated that TIF interacts most strongly with a sequence centered at -29 and less tightly with sequences upstream and downstream. Some alterations of the base sequence closer to the transcription start site (and outside the TIF-protected site) also significantly decreased specific RNA synthesis in vitro. These were within the region which is protected from DNase I digestion by polymerase I, but these mutations did not detectably affect the binding of polymerase to the promoter.

scholarly journals Two RNA Polymerase I Subunits Control the Binding and Release of Rrn3 during Transcription

2007 ◽  
Vol 28 (5) ◽  
pp. 1596-1605 ◽  
Author(s):  
Frédéric Beckouet ◽  
Sylvie Labarre-Mariotte ◽  
Benjamin Albert ◽  
Yukiko Imazawa ◽  
Michel Werner ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Transcription Initiation ◽  
Binding Domain ◽  
Rna Polymerase I ◽  
Initiation Factor ◽  
C Terminus ◽  
Transcription Initiation Factor ◽  
Polymerase I ◽  
Polymerase Mutants

ABSTRACT Rpa34 and Rpa49 are nonessential subunits of RNA polymerase I, conserved in species from Saccharomyces cerevisiae and Schizosaccharomyces pombe to humans. Rpa34 bound an N-terminal region of Rpa49 in a two-hybrid assay and was lost from RNA polymerase in an rpa49 mutant lacking this Rpa34-binding domain, whereas rpa34Δ weakened the binding of Rpa49 to RNA polymerase. rpa34Δ mutants were caffeine sensitive, and the rpa34Δ mutation was lethal in a top1Δ mutant and in rpa14Δ, rpa135(L656P), and rpa135(D395N) RNA polymerase mutants. These defects were shared by rpa49Δ mutants, were suppressed by the overexpression of Rpa49, and thus, were presumably mediated by Rpa49 itself. rpa49 mutants lacking the Rpa34-binding domain behaved essentially like rpa34Δ mutants, but strains carrying rpa49Δ and rpa49-338::HIS3 (encoding a form of Rpa49 lacking the conserved C terminus) had reduced polymerase occupancy at 30°C, failed to grow at 25°C, and were sensitive to 6-azauracil and mycophenolate. Mycophenolate almost fully dissociated the mutant polymerase from its ribosomal DNA (rDNA) template. The rpa49Δ and rpa49-338::HIS3 mutations had a dual effect on the transcription initiation factor Rrn3 (TIF-IA). They partially impaired its recruitment to the rDNA promoter, an effect that was bypassed by an N-terminal deletion of the Rpa43 subunit encoded by rpa43-35,326, and they strongly reduced the release of the Rrn3 initiation factor during elongation. These data suggest a dual role of the Rpa49-Rpa34 dimer during the recruitment of Rrn3 and its subsequent dissociation from the elongating polymerase.

scholarly journals Inhibition of TATA Binding Protein Dimerization by RNA Polymerase III Transcription Initiation Factor Brf1

2004 ◽  
Vol 279 (31) ◽  
pp. 32401-32406 ◽  
Author(s):  
Diane E. Alexander ◽  
David J. Kaczorowski ◽  
Amy J. Jackson-Fisher ◽  
Drew M. Lowery ◽  
Sara J. Zanton ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Transcription Initiation ◽  
Binding Protein ◽  
Rna Polymerase Iii ◽  
Tata Binding Protein ◽  
Initiation Factor ◽  
Protein Dimerization ◽  
Polymerase Iii ◽  
Transcription Initiation Factor

Events during eucaryotic rRNA transcription initiation and elongation: conversion from the closed to the open promoter complex requires nucleotide substrates

1988 ◽  
Vol 8 (5) ◽  
pp. 1940-1946
Author(s):  
E Bateman ◽  
M R Paule
Keyword(s):  
Rna Polymerase ◽  
Transcription Initiation ◽  
Topological Analysis ◽  
Acanthamoeba Castellanii ◽  
Rna Polymerase I ◽  
Initiation Factor ◽  
Rrna Transcription ◽  
Promoter Complex ◽  
Polymerase I

Chemical footprinting and topological analysis were carried out on the Acanthamoeba castellanii rRNA transcription initiation factor (TIF) and RNA polymerase I complexes with DNA during transcription initiation and elongation. The results show that the binding of TIF and polymerase to the promoter does not alter the supercoiling of the DNA template and the template does not become sensitive to modification by diethylpyrocarbonate, which can identify melted DNA regions. Thus, in contrast to bacterial RNA polymerase, the eucaryotic RNA polymerase I-promoter complex is in a closed configuration preceding addition of nucleotides in vitro. Initiation and 3'-O-methyl CTP-limited translocation by RNA polymerase I results in separation of the polymerase-TIF footprints, leaving the TIF footprint unaltered. In contrast, initiation and translocation result in a significant change in the conformation of the polymerase-DNA complex, culminating in an unwound DNA region of at least 10 base pairs.

scholarly journals Binding of YY1 to a site overlapping a weak TATA box is essential for transcription from the uteroglobin promoter in endometrial cells.

1996 ◽  
Vol 16 (11) ◽  
pp. 6398-6407 ◽  
Author(s):  
J Klug ◽  
M Beato
Keyword(s):  
Cell Lines ◽  
Transcription Initiation ◽  
Binding Protein ◽  
Cell Types ◽  
Tata Box ◽  
Initiation Factor ◽  
Clara Cells ◽  
Endometrial Cells ◽  
Tata Box Binding Protein

The gene for rabbit uteroglobin codes for a small calcium-, steroid-, and biphenyl metabolite-binding homodimeric protein which is expressed in a variety of epithelial cell types such as Clara cells (lung) and the glandular and luminal cells of the endometrium. One important region mediating its efficient transcription in a human endometrium-derived cell line, Ishikawa, is centered around a noncanonical TATA box. Two factors, TATA core factor (TCF), expressed in cell lines derived from uteroglobin-expressing tissues, and the ubiquitously expressed TATA palindrome factor, bind to the DNA major groove at two adjacent sites within this region. Here, we report the identification of the TATA palindrome factor as the transcription/initiation factor YY1 by microsequencing of the biochemically purified factor from HeLa cells. The binding site for YY1 within the uteroglobin gene is unique in its sequence and its location overlapping a weak TATA box (TACA). Binding of YY1 was required for efficient transcription in TCF-positive Ishikawa cells, which responded only weakly to a change of TACA to TATA, although in vitro binding affinity for the TATA-box-binding protein increased by 1 order of magnitude. In contrast, in CV-1 cells, lacking TCF, binding of YY1 was not required for transcription in the context of a wild-type TACA box, whereas a change from TACA to TATA led to significantly increased reporter gene expression. DNA binding data exclude a role of YY1 in stabilizing the interaction of the TATA-box-binding protein with the uteroglobin promoter. We conclude that cell lines derived from uteroglobin-expressing tissues overcome the weak TATA box with the help of auxiliary factors, one of them being YY1.

scholarly journals Mitochondrial ubiquinone–mediated longevity is marked by reduced cytoplasmic mRNA translation

2018 ◽  
Vol 1 (5) ◽  
pp. e201800082 ◽  
Author(s):  
Marte Molenaars ◽  
Georges E Janssens ◽  
Toon Santermans ◽  
Marco Lezzerini ◽  
Rob Jelier ◽  
...  
Keyword(s):  
Insulin Signaling ◽  
Transcription Initiation ◽  
Binding Protein ◽  
Mrna Translation ◽  
Tata Binding Protein ◽  
Early Embryogenesis ◽  
Life Extension ◽  
Initiation Factor ◽  
Associated Factor ◽  
Transcription Initiation Factor

Mutations in the clk-1 gene impair mitochondrial ubiquinone biosynthesis and extend the lifespan in Caenorhabditis elegans. We demonstrate here that this life extension is linked to the repression of cytoplasmic mRNA translation, independent of the alleged nuclear form of CLK-1. Clk-1 mutations inhibit polyribosome formation similarly to daf-2 mutations that dampen insulin signaling. Comparisons of total versus polysomal RNAs in clk-1(qm30) mutants reveal a reduction in the translational efficiencies of mRNAs coding for elements of the translation machinery and an increase in those coding for the oxidative phosphorylation and autophagy pathways. Knocking down the transcription initiation factor TATA-binding protein-associated factor 4, a protein that becomes sequestered in the cytoplasm during early embryogenesis to induce transcriptional silencing, ameliorates the clk-1 inhibition of polyribosome formation. These results underscore a prominent role for the repression of cytoplasmic protein synthesis in eukaryotic lifespan extension and suggest that mutations impairing mitochondrial function are able to exploit this repression similarly to reductions of insulin signaling. Moreover, this report reveals an unexpected role for TATA-binding protein-associated factor 4 as a repressor of polyribosome formation when ubiquinone biosynthesis is compromised.

scholarly journals The NF-κB Nucleolar Stress Response Pathway

Biomedicines ◽  
2021 ◽  
Vol 9 (9) ◽  
pp. 1082
Author(s):  
Hazel C. Thoms ◽  
Lesley A. Stark
Keyword(s):  
Stress Response ◽  
Transcription Initiation ◽  
Critical Role ◽  
Initiation Factor ◽  
Downstream Effector ◽  
Nucleolar Stress ◽  
Transcription Initiation Factor ◽  
Stress Response Pathway ◽  
Regulate Cell Growth ◽  
Polymerase I

The nuclear organelle, the nucleolus, plays a critical role in stress response and the regulation of cellular homeostasis. P53 as a downstream effector of nucleolar stress is well defined. However, new data suggests that NF-κB also acts downstream of nucleolar stress to regulate cell growth and death. In this review, we will provide insight into the NF-κB nucleolar stress response pathway. We will discuss apoptosis mediated by nucleolar sequestration of RelA and new data demonstrating a role for p62 (sequestosome (SQSTM1)) in this process. We will also discuss activation of NF-κB signalling by degradation of the RNA polymerase I (PolI) complex component, transcription initiation factor-IA (TIF-IA (RRN3)), and contexts where TIF-IA-NF-κB signalling may be important. Finally, we will discuss how this pathway is targeted by aspirin to mediate apoptosis of colon cancer cells.

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