scholarly journals RNA polymerase II condensate formation and association with Cajal and histone locus bodies in living human cells

2021 ◽  
Author(s):  
Takashi Imada ◽  
Takeshi Shimi ◽  
Ai Kaiho ◽  
Yasushi Saeki ◽  
Hiroshi Kimura
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Human Cells ◽  
Histone Locus Bodies ◽  
Condensate Formation ◽  
Histone Locus

scholarly journals RNA polymerase II condensate formation and association with Cajal and histone locus bodies in living human cells

2020 ◽  
Author(s):  
Takashi Imada ◽  
Takeshi Shimi ◽  
Ai Kaiho ◽  
Yasushi Saeki ◽  
Hiroshi Kimura
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Gene Clusters ◽  
Nuclear Bodies ◽  
Histone Genes ◽  
Small Nuclear Rna ◽  
Pol Ii ◽  
Histone Locus Bodies ◽  
Dynamic Structures ◽  
Histone Locus

ABSTRACTIn eukaryotic nuclei, a number of phase-separated nuclear bodies (NBs) are present. RNA polymerase II (Pol II) is the main player in transcription and forms large condensates in addition to localizing at numerous transcription foci. Cajal bodies (CBs) and histone locus bodies (HLBs) are NBs that are involved in transcriptional and post-transcriptional regulation of small nuclear RNA and histone genes. By live-cell imaging using human HCT116 cells, we here show that Pol II condensates (PCs) nucleated near CBs and HLBs, and the number of PCs increased during S phase concomitantly with the activation period of histone genes. Ternary PC–CB– HLB associates were formed via three pathways: nucleation of PCs and HLBs near CBs, interaction between preformed PC–HLBs with CBs, and nucleation of PCs near preformed CB– HLBs. Coilin knockout increased the co-localization rate between PCs and HLBs, whereas the number, nucleation timing, and phosphorylation status of PCs remained unchanged. Depletion of PCs did not affect CBs and HLBs. Treatment with 1,6-hexanediol revealed that PCs were more liquid-like than CBs and HLBs. Thus, PCs are dynamic structures often nucleated following the activation of gene clusters associated with other NBs. (187 words)

scholarly journals Inhibition of RNA polymerase II transcription in human cells by synthetic DNA-binding ligands

1998 ◽  
Vol 95 (22) ◽  
pp. 12890-12895 ◽  
Author(s):  
L. A. Dickinson ◽  
R. J. Gulizia ◽  
J. W. Trauger ◽  
E. E. Baird ◽  
D. E. Mosier ◽  
...  
Keyword(s):  
Dna Binding ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Human Cells ◽  
Synthetic Dna ◽  
Rna Polymerase Ii Transcription

scholarly journals ELA1 and CUL3 Are Required Along with ELC1 for RNA Polymerase II Polyubiquitylation and Degradation in DNA-Damaged Yeast Cells

2007 ◽  
Vol 27 (8) ◽  
pp. 3211-3216 ◽  
Author(s):  
Balazs Ribar ◽  
Louise Prakash ◽  
Satya Prakash
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Ubiquitin Ligase ◽  
Ring Finger ◽  
Human Cells ◽  
Yeast Cells ◽  
Pol Ii ◽  
Von Hippel Lindau ◽  
Ubiquitin Ligase E3 ◽  
Cullin 3

ABSTRACT Treatment of yeast and human cells with DNA-damaging agents elicits lysine 48-linked polyubiquitylation of Rpb1, the largest subunit of RNA polymerase II (Pol II), which targets Pol II for proteasomal degradation. However, the ubiquitin ligase (E3) responsible for Pol II polyubiquitylation has not been identified in humans or the yeast Saccharomyces cerevisiae . Here we show that elongin A (Ela1) and cullin 3 (Cul3) are required for Pol II polyubiquitylation and degradation in yeast cells, and on the basis of these and other observations, we propose that an E3 comprised of elongin C (Elc1), Ela1, Cul3, and the RING finger protein Roc1 (Rbx1) mediates this process in yeast cells. This study provides, in addition to the identification of the E3 required for Pol II polyubiquitylation and degradation in yeast cells, the first evidence for a specific function in yeast for a member of the elongin C/BC-box protein/cullin family of ligases. Also, these observations raise the distinct possibility that the elongin C-containing ubiquitin ligase, the von Hippel-Lindau tumor suppressor complex, promotes Pol II polyubiquitylation and degradation in human cells.

scholarly journals Baculovirus P35 interacts with a subunit of human RNA polymerase II and can enhance promoter activity in human cells

2003 ◽  
Vol 84 (11) ◽  
pp. 3011-3019 ◽  
Author(s):  
David Takramah ◽  
Barbara M. Seiffert ◽  
Sophie Schaller ◽  
Marc Vigneron ◽  
Georg Häcker
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Promoter Activity ◽  
Human Cells ◽  
A Subunit ◽  
Baculovirus P35 ◽  
Enhance Promoter Activity

scholarly journals Integrator Subunit 4 is a ‘Symplekin-like’ Scaffold that Associates with INTS9/11 to Form the Integrator Cleavage Module

2017 ◽  
Author(s):  
Todd R. Albrecht ◽  
Sergey P. Shevtsov ◽  
Lauren G. Mascibroda ◽  
Natoya J. Peart ◽  
Iain A. Sawyer ◽  
...  
Keyword(s):  
Rna Polymerase Ii ◽  
Cajal Body ◽  
Catalytic Core ◽  
Histone Locus Bodies ◽  
Transcriptional Regulatory ◽  
Significant Homology ◽  
Regulatory Complex ◽  
Cleavage And Polyadenylation ◽  
Histone Locus ◽  
Β Sheet

AbstractIntegrator (INT) is a transcriptional regulatory complex associated with RNA polymerase II that is required for the 3’-end processing of both UsnRNAs and enhancer RNAs. Integrator subunits 9 (INTS9) and INTS11 constitute the catalytic core of INT and are paralogues of the cleavage and polyadenylation specificity factors CPSF100 and CPSF73. While CPSF73/100 are known to associate with a third protein called Symplekin, there is no paralog of Symplekin within INT raising the question of how INTS9/11 associate with the other INT subunits. Here, we have identified that INTS4 is a specific and conserved interaction partner of INTS9/11 that does not interact with either subunit individually. Although INTS4 has no significant homology with Symplekin, it possesses N-terminal HEAT repeats similar to Symplekin but also contains a β-sheet rich C-terminal region, both of which are important to bind INTS9/11. We assess three functions of INT including UsnRNA 3’-end processing, maintenance of Cajal body integrity, and formation of histone locus bodies to conclude that INTS4/9/11 are the most critical of the INT subunits for UsnRNA biogenesis. Altogether, these results indicate that INTS4/9/11 compose a heterotrimeric complex that likely represents the Integrator ‘cleavage module’ responsible for its endonucleolytic activity.

Fixation-induced redistribution of hyperphosphorylated RNA polymerase II in the nucleus of human cells

2004 ◽  
Vol 295 (2) ◽  
pp. 460-468 ◽  
Author(s):  
Pascale V. Guillot ◽  
Sheila Q. Xie ◽  
Michael Hollinshead ◽  
Ana Pombo
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Human Cells

Early Effects of Topoisomerase I Inhibition on RNA Polymerase II Along Transcribed Genes in Human Cells

2006 ◽  
Vol 357 (1) ◽  
pp. 127-138 ◽  
Author(s):  
Andriy Khobta ◽  
Francesca Ferri ◽  
Luca Lotito ◽  
Alessandra Montecucco ◽  
Rossella Rossi ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Topoisomerase I ◽  
Human Cells ◽  
Early Effects
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