Corrigendum to “Regulation of RNA Polymerase III Transcription by Maf1 in Mammalian Cells” [J. Mol. Biol. 378(3) (2008) 481–491]

Abstract Background Chromatin organization is central to precise control of gene expression. In various eukaryotic species, domains of pervasive cis-chromatin interactions demarcate functional domains of the genomes. In nematode Caenorhabditis elegans, however, pervasive chromatin contact domains are limited to the dosage-compensated sex chromosome, leaving the principle of C. elegans chromatin organization unclear. Transcription factor III C (TFIIIC) is a basal transcription factor complex for RNA polymerase III, and is implicated in chromatin organization. TFIIIC binding without RNA polymerase III co-occupancy, referred to as extra-TFIIIC binding, has been implicated in insulating active and inactive chromatin domains in yeasts, flies, and mammalian cells. Whether extra-TFIIIC sites are present and contribute to chromatin organization in C. elegans remains unknown. Results We identified 504 TFIIIC-bound sites absent of RNA polymerase III and TATA-binding protein co-occupancy characteristic of extra-TFIIIC sites in C. elegans embryos. Extra-TFIIIC sites constituted half of all identified TFIIIC binding sites in the genome. Extra-TFIIIC sites formed dense clusters in cis. The clusters of extra-TFIIIC sites were highly over-represented within the distal arm domains of the autosomes that presented a high level of heterochromatin-associated histone H3K9 trimethylation (H3K9me3). Furthermore, extra-TFIIIC clusters were embedded in the lamina-associated domains. Despite the heterochromatin environment of extra-TFIIIC sites, the individual clusters of extra-TFIIIC sites were devoid of and resided near the individual H3K9me3-marked regions. Conclusion Clusters of extra-TFIIIC sites were pervasive in the arm domains of C. elegans autosomes, near the outer boundaries of H3K9me3-marked regions. Given the reported activity of extra-TFIIIC sites in heterochromatin insulation in yeasts, our observation raised the possibility that TFIIIC may also demarcate heterochromatin in C. elegans.

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CK2 Forms a Stable Complex with TFIIIB and Activates RNA Polymerase III Transcription in Human Cells

Molecular and Cellular Biology ◽

10.1128/mcb.22.11.3757-3768.2002 ◽

2002 ◽

Vol 22 (11) ◽

pp. 3757-3768 ◽

Cited By ~ 53

Author(s):

Imogen M. Johnston ◽

Simon J. Allison ◽

Jennifer P. Morton ◽

Laura Schramm ◽

Pamela H. Scott ◽

...

Keyword(s):

Rna Polymerase ◽

Mammalian Cells ◽

Rna Polymerase Iii ◽

Stable Complex ◽

Class Iii ◽

Potent Effect ◽

Cell Extracts ◽

Polymerase Iii ◽

Chemical Inhibitors

ABSTRACT CK2 is a highly conserved protein kinase with growth-promoting and oncogenic properties. It is known to activate RNA polymerase III (PolIII) transcription in Saccharomyces cerevisiae and is shown here to also exert a potent effect on PolIII in mammalian cells. Peptide and chemical inhibitors of CK2 block PolIII transcription in human cell extracts. Furthermore, PolIII transcription in mammalian fibroblasts is decreased significantly when CK2 activity is compromised by chemical inhibitors, antisense oligonucleotides, or kinase-inactive mutants. Coimmunoprecipitation and cofractionation show that endogenous human CK2 associates stably and specifically with the TATA-binding protein-containing factor TFIIIB, which brings PolIII to the initiation site of all class III genes. Serum stimulates TFIIIB phosphorylation in vivo, an effect that is diminished by inhibitors of CK2. Binding to TFIIIC2 recruits TFIIIB to most PolIII promoters; this interaction is compromised specifically by CK2 inhibitors. The data suggest that CK2 stimulates PolIII transcription by binding and phosphorylating TFIIIB and facilitating its recruitment by TFIIIC2. CK2 also activates PolI transcription in mammals and may therefore provide a mechanism to coregulate the output of PolI and PolIII. CK2 provides a rare example of an endogenous activity that operates on the PolIII system in both mammals and yeasts. Such evolutionary conservation suggests that this control may be of fundamental importance.

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Transcription Factors of RNA Polymerase III from Mammalian Cells

Activation of Hormone and Growth Factor Receptors ◽

10.1007/978-94-009-1936-5_12 ◽

1990 ◽

pp. 119-136

Author(s):

Klaus Seifart ◽

Rainer Waldschmidt ◽

Harald Schneider

Keyword(s):

Transcription Factors ◽

Rna Polymerase ◽

Mammalian Cells ◽

Rna Polymerase Iii ◽

Polymerase Iii

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Regulated expression of functional external guide sequences in mammalian cells using a U6 RNA polymerase III promoter

RNA ◽

10.1261/rna.2140505 ◽

2005 ◽

Vol 11 (10) ◽

pp. 1588-1595 ◽

Cited By ~ 3

Author(s):

E. KOVRIGINA

Keyword(s):

Rna Polymerase ◽

Mammalian Cells ◽

Rna Polymerase Iii ◽

Polymerase Iii ◽

Regulated Expression ◽

U6 Rna

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Transcription-independent TFIIIC-bound sites cluster near heterochromatin boundaries within lamina-associated domains in C. elegans

10.1101/813642 ◽

2019 ◽

Author(s):

Alexis V. Stutzman ◽

April S. Liang ◽

Vera Beilinson ◽

Kohta Ikegami

Keyword(s):

Transcription Factor ◽

Rna Polymerase ◽

Mammalian Cells ◽

Sex Chromosome ◽

Rna Polymerase Iii ◽

Chromatin Organization ◽

Control Of Gene Expression ◽

C Elegans ◽

Polymerase Iii ◽

The Individual

ABSTRACTBACKGROUNDChromatin organization is central to precise control of gene expression. In various eukaryotic spieces, domains of pervasive cis-chromatin interactions demarcate functional domains of the genomes. In nematode C. elegans, however, pervasive chromatin contact domains are limited to the dosage-compensated sex chromosome, leaving the principle of C. elegans chromatin organization unclear. Transcription Factor III C (TFIIIC) is a basal transcription factor complex for RNA Polymerase III, and is implicated in chromatin organization. TFIIIC binding without RNA Polymerase III co-occupancy, referred to as extra-TFIIIC binding, has been implicated in insulating active and inactive chromatin domains in yeasts, flies, and mammalian cells. Whether extra-TFIIIC sites are present and contribute to chromatin organization in C. elegans remains unknown.RESULTSWe identified 504 TFIIIC-bound sites absent of RNA Polymerase III and TATA-binding protein co-occupancy characteristic of extra-TFIIIC sites in C. elegans embryos. Extra-TFIIIC sites constituted half of all identified TFIIIC binding sites in the genome. Extra-TFIIIC sites formed dense clusters in cis. The clusters of extra-TFIIIC sites were highly over-represented within the distal arm domains of the autosomes that presented a high level of heterochromatin-associated histone H3K9 trimethylation (H3K9me3). Furthermore, extra-TFIIIC clusters were embedded in the lamina-associated domains. Despite the heterochromatin environment of extra-TFIIIC sites, the individual clusters of extra-TFIIIC sites were devoid of and resided near the individual H3K9me3-marked regions.CONCLUSIONClusters of extra-TFIIIC sites were pervasive in the arm domains of C. elegans autosomes, near the outer boundaries of H3K9me3-marked regions. Given the reported activity of extra-TFIIIC sites in heterochromatin insulation in yeasts, our observation raised the possibility that TFIIIC may also demarcate heterochromatin in C. elegans.

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Ro small cytoplasmic ribonucleoproteins are a subclass of La ribonucleoproteins: further characterization of the Ro and La small ribonucleoproteins from uninfected mammalian cells

Molecular and Cellular Biology ◽

10.1128/mcb.1.12.1138-1149.1981 ◽

1981 ◽

Vol 1 (12) ◽

pp. 1138-1149

Author(s):

J P Hendrick ◽

S L Wolin ◽

J Rinke ◽

M R Lerner ◽

J A Steitz

Keyword(s):

Rna Polymerase ◽

Mammalian Cells ◽

Protein Complexes ◽

Rna Polymerase Iii ◽

Protein S ◽

Human Cells ◽

Rna Molecules ◽

Transcription System ◽

Polymerase Iii ◽

La Protein

Small ribonucleic acid (RNA)-protein complexes precipitated by anti-Ro and anti-La antibodies from lupus patients have been examined with emphasis on their RNA components. In both ribonucleoprotein (RNP) classes, the numbers of different RNA molecules and their sequences vary between mouse and human cells. The complex mixtures of La RNAs include two previously sequenced 4.5S RNAs from mouse cells and 5S ribosomal RNA-like molecules from both mouse and human cells. All Ro and La RNAs possess 5-triphosphates. Some La RNAs have internal modifications typical of transfer RNAs. The Ro RNPs are quite stable and are localized by immunofluorescence in the cell cytoplasm, whereas the majority of the La RNPs turn over rapidly and reside in the nucleus. Despite these differences, reconstitution experiments show that the Ro particles carry the La as well as the Ro determinant. Studies using a nuclear transcription system demonstrate that most of the La RNAs are synthesized by RNA polymerase III. The possibility that the La protein(s) functions in the transcription or maturation of all RNA polymerase III transcripts is discussed.

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Ro small cytoplasmic ribonucleoproteins are a subclass of La ribonucleoproteins: further characterization of the Ro and La small ribonucleoproteins from uninfected mammalian cells.

Molecular and Cellular Biology ◽

10.1128/mcb.1.12.1138 ◽

1981 ◽

Vol 1 (12) ◽

pp. 1138-1149 ◽

Cited By ~ 240

Author(s):

J P Hendrick ◽

S L Wolin ◽

J Rinke ◽

M R Lerner ◽

J A Steitz

Keyword(s):

Rna Polymerase ◽

Mammalian Cells ◽

Protein Complexes ◽

Rna Polymerase Iii ◽

Protein S ◽

Human Cells ◽

Rna Molecules ◽

Transcription System ◽

Polymerase Iii ◽

La Protein

Small ribonucleic acid (RNA)-protein complexes precipitated by anti-Ro and anti-La antibodies from lupus patients have been examined with emphasis on their RNA components. In both ribonucleoprotein (RNP) classes, the numbers of different RNA molecules and their sequences vary between mouse and human cells. The complex mixtures of La RNAs include two previously sequenced 4.5S RNAs from mouse cells and 5S ribosomal RNA-like molecules from both mouse and human cells. All Ro and La RNAs possess 5-triphosphates. Some La RNAs have internal modifications typical of transfer RNAs. The Ro RNPs are quite stable and are localized by immunofluorescence in the cell cytoplasm, whereas the majority of the La RNPs turn over rapidly and reside in the nucleus. Despite these differences, reconstitution experiments show that the Ro particles carry the La as well as the Ro determinant. Studies using a nuclear transcription system demonstrate that most of the La RNAs are synthesized by RNA polymerase III. The possibility that the La protein(s) functions in the transcription or maturation of all RNA polymerase III transcripts is discussed.

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Functions of paralogous RNA polymerase III subunits POLR3G and POLR3GL in mouse development

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.1922821117 ◽

2020 ◽

Vol 117 (27) ◽

pp. 15702-15711

Author(s):

Xiaoling Wang ◽

Alan Gerber ◽

Wei-Yi Chen ◽

Robert G. Roeder

Keyword(s):

Rna Polymerase ◽

Knockout Mice ◽

Mammalian Cells ◽

Target Genes ◽

Rna Polymerase Iii ◽

Embryonic Stem ◽

Mouse Development ◽

Polymerase Iii ◽

Pol Iii

Mammalian cells contain two isoforms of RNA polymerase III (Pol III) that differ in only a single subunit, with POLR3G in one form (Pol IIIα) and the related POLR3GL in the other form (Pol IIIβ). Previous research indicates that POLR3G and POLR3GL are differentially expressed, with POLR3G expression being highly enriched in embryonic stem cells (ESCs) and tumor cells relative to the ubiquitously expressed POLR3GL. To date, the functional differences between these two subunits remain largely unexplored, especially in vivo. Here, we show that POLR3G and POLR3GL containing Pol III complexes bind the same target genes and assume the same functions both in vitro and in vivo and, to a significant degree, can compensate for each other in vivo. Notably, an observed defect in the differentiation ability of POLR3G knockout ESCs can be rescued by exogenous expression of POLR3GL. Moreover, whereas POLR3G knockout mice die at a very early embryonic stage, POLR3GL knockout mice complete embryonic development without noticeable defects but die at about 3 wk after birth with signs of both general growth defects and potential cerebellum-related neuronal defects. The different phenotypes of the knockout mice likely reflect differential expression levels of POLR3G and POLR3GL across developmental stages and between tissues and insufficient amounts of total Pol III in vivo.

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