scholarly journals Turnover and Function of Noncoding RNA Polymerase II Transcripts

2006 ◽  
Vol 71 (0) ◽  
pp. 275-284 ◽  
Author(s):  
M.J. DYE ◽  
N. GROMAK ◽  
D. HAUSSECKER ◽  
S. WEST ◽  
N.J. PROUDFOOT
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Noncoding Rna ◽  
And Function

scholarly journals Human RNA polymerase II subunit hsRPB7 functions in yeast and influences stress survival and cell morphology.

1995 ◽  
Vol 6 (7) ◽  
pp. 759-775 ◽  
Author(s):  
V Khazak ◽  
P P Sadhale ◽  
N A Woychik ◽  
R Brent ◽  
E A Golemis
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Specific Pattern ◽  
Yeast Cells ◽  
Human Genes ◽  
Complete Set ◽  
High And Low Temperatures ◽  
And Function ◽  
Two Hybrid ◽  
Potential Regulatory Role

Using a screen to identify human genes that promote pseudohyphal conversion in Saccharomyces cerevisiae, we obtained a cDNA encoding hsRPB7, a human homologue of the seventh largest subunit of yeast RNA polymerase II (RPB7). Overexpression of yeast RPB7 in a comparable strain background caused more pronounced cell elongation than overexpression of hsRPB7. hsRPB7 sequence and function are strongly conserved with its yeast counterpart because its expression can rescue deletion of the essential RPB7 gene at moderate temperatures. Further, immuno-precipitation of RNA polymerase II from yeast cells containing hsRPB7 revealed that the hsRPB7 assembles the complete set of 11 other yeast subunits. However, at temperature extremes and during maintenance at stationary phase, hsRPB7-containing yeast cells lose viability rapidly, stress-sensitive phenotypes reminiscent of those associated with deletion of the RPB4 subunit with which RPB7 normally complexes. Two-hybrid analysis revealed that although hsRPB7 and RPB4 interact, the association is of lower affinity than the RPB4-RPB7 interaction, providing a probable mechanism for the failure of hsRPB7 to fully function in yeast cells at high and low temperatures. Finally, surprisingly, hsRPB7 RNA in human cells is expressed in a tissue-specific pattern that differs from that of the RNA polymerase II largest subunit, implying a potential regulatory role for hsRPB7. Taken together, these results suggest that some RPB7 functions may be analogous to those possessed by the stress-specific prokaryotic sigma factor rpoS.

scholarly journals Domains in the SPT5 Protein That Modulate Its Transcriptional Regulatory Properties

2000 ◽  
Vol 20 (9) ◽  
pp. 2970-2983 ◽  
Author(s):  
Dmitri Ivanov ◽  
Youn Tae Kwak ◽  
Jun Guo ◽  
Richard B. Gaynor
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Transcriptional Repression ◽  
Transcriptional Elongation ◽  
Tat Protein ◽  
C Terminus ◽  
Heptad Repeats ◽  
And Function ◽  
Hiv 1

ABSTRACT SPT5 and its binding partner SPT4 regulate transcriptional elongation by RNA polymerase II. SPT4 and SPT5 are involved in both 5,6-dichloro-1-β-d-ribofuranosylbenzimidazole (DRB)-mediated transcriptional inhibition and the activation of transcriptional elongation by the human immunodeficiency virus type 1 (HIV-1) Tat protein. Recent data suggest that P-TEFb, which is composed of CDK9 and cyclin T1, is also critical in regulating transcriptional elongation by SPT4 and SPT5. In this study, we analyze the domains of SPT5 that regulate transcriptional elongation in the presence of either DRB or the HIV-1 Tat protein. We demonstrate that SPT5 domains that bind SPT4 and RNA polymerase II, in addition to a region in the C terminus of SPT5 that contains multiple heptad repeats and is designated CTR1, are critical for in vitro transcriptional repression by DRB and activation by the Tat protein. Furthermore, the SPT5 CTR1 domain is a substrate for P-TEFb phosphorylation. These results suggest that C-terminal repeats in SPT5, like those in the RNA polymerase II C-terminal domain, are sites for P-TEFb phosphorylation and function in modulating its transcriptional elongation properties.

scholarly journals ARS2 Regulates Nuclear Paraspeckle Formation through 3′-End Processing and Stability of NEAT1 Long Noncoding RNA

2019 ◽  
Vol 40 (4) ◽  
Author(s):  
Mitsuhiro Machitani ◽  
Ichiro Taniguchi ◽  
Mutsuhito Ohno
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Rna Processing ◽  
Long Noncoding Rna ◽  
Crucial Role ◽  
Noncoding Rna ◽  
Subsequent Formation ◽  
Factor I ◽  
Cap Binding Complex ◽  
Resistance Protein

ABSTRACT Nuclear paraspeckle assembly transcript 1 (NEAT1) is a long noncoding RNA that functions as an essential framework of subnuclear paraspeckle bodies. Of the two isoforms (NEAT1_1 and NEAT1_2) produced by alternative 3′-end RNA processing, the longer isoform, NEAT1_2, plays a crucial role in paraspeckle formation. Here, we demonstrate that the 3′-end processing and stability of NEAT1 RNAs are regulated by arsenic resistance protein 2 (ARS2), a factor interacting with the cap-binding complex (CBC) that binds to the m7G cap structure of RNA polymerase II transcripts. The knockdown of ARS2 inhibited the association between NEAT1 and mammalian cleavage factor I (CFIm), which produces the shorter isoform, NEAT1_1. Furthermore, the knockdown of ARS2 led to the preferential stabilization of NEAT1_2. As a result, NEAT1_2 RNA levels were markedly elevated in ARS2 knockdown cells, leading to an increase in the number of paraspeckles. These results reveal a suppressive role for ARS2 in NEAT1_2 expression and the subsequent formation of paraspeckles.

scholarly journals RNA polymerase II CTD interactome with 3′ processing and termination factors in fission yeast and its impact on phosphate homeostasis

2018 ◽  
Vol 115 (45) ◽  
pp. E10652-E10661 ◽  
Author(s):  
Ana M. Sanchez ◽  
Stewart Shuman ◽  
Beate Schwer
Keyword(s):  
Gene Expression ◽  
Rna Polymerase ◽  
Fission Yeast ◽  
Rna Polymerase Ii ◽  
Noncoding Rna ◽  
Synthetically Lethal ◽  
Heptad Repeats ◽  
Carboxy Terminal ◽  
Key Steps ◽  
Rna Polymerase Ii Ctd

The carboxy-terminal domain (CTD) code encrypted within the Y1S2P3T4S5P6S7heptad repeats of RNA polymerase II (Pol2) is deeply rooted in eukaryal biology. Key steps to deciphering the code are identifying the events in gene expression that are governed by individual “letters” and then defining a vocabulary of multiletter “words” and their meaning. Thr4 and Ser7 exert opposite effects on the fission yeastpho1gene, expression of which is repressed under phosphate-replete conditions by transcription of an upstream flanking long noncoding RNA (lncRNA). Here we attribute the derepression ofpho1by a CTD-S7Amutation to precocious termination of lncRNA synthesis, an effect that is erased by mutations of cleavage-polyadenylation factor (CPF) subunits Ctf1, Ssu72, Ppn1, Swd22, and Dis2 and termination factor Rhn1. By contrast, a CTD-T4Amutation hyperrepressespho1, as do CPF subunit and Rhn1 mutations, implying thatT4Areduces lncRNA termination. Moreover, CTD-T4Ais synthetically lethal withppn1∆ andswd22∆, signifying that Thr4 and the Ppn1•Swd22 module play important, functionally redundant roles in promoting Pol2 termination. We find that Ppn1 and Swd22 become essential for viability when the CTD array is curtailed and thatS7Aovercomes the need for Ppn1•Swd22 in the short CTD context. Mutational synergies highlight redundant essential functions of (i) Ppn1•Swd22 and Rhn1, (ii) Ppn1•Swd22 and Ctf1, and (iii) Ssu72 and Dis2 phosphatases. CTD allelesY1F,S2A, andT4Ahave overlapping synthetic lethalities withppn1∆ andswd22∆, suggesting that Tyr1-Ser2-Thr4 form a three-letter CTD word that abets termination, with Rhn1 being a likely “reader” of this word.

Cardiomyocyte-specific loss of RNA polymerase II subunit 5-mediating protein causes myocardial dysfunction and heart failure

2018 ◽  
Vol 115 (11) ◽  
pp. 1617-1628
Author(s):  
Jian Zhang ◽  
Jingyi Sheng ◽  
Liwei Dong ◽  
Yinli Xu ◽  
Liming Yu ◽  
...  
Keyword(s):  
Heart Failure ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Genome Stability ◽  
Transforming Growth Factor ◽  
Myocardial Dysfunction ◽  
Transforming Growth Factor Β ◽  
And Function ◽  
Deficient Mice

AbstractAimsMyocardial dysfunction is an important cause of heart failure (HF). RNA polymerase II subunit 5 (RPB5)-mediating protein (RMP) is a transcriptional mediating protein which co-ordinates cellular processes including gene expression, metabolism, proliferation, and genome stability. However, its role in cardiac disease remains unknown. We aimed to determine the role and regulatory mechanisms of RMP in cardiomyocyte function and the development of HF.Methods and resultsMyocardial RMP expression was examined in human heart tissues from healthy controls and patients with advanced HF. Compared to normal cardiac tissues, RMP levels were significantly decreased in the myocardium of patients with advanced HF. To investigate the role of RMP in cardiac function, Cre-loxP recombinase technology was used to generate tamoxifen-inducible cardiomyocyte-specific Rmp knockout mice. Unexpectedly, cardiomyocyte-specific deletion of Rmp in mice resulted in contractile dysfunction, cardiac dilatation, and fibrosis. Furthermore, the lifespan of cardiac-specific Rmp-deficient mice was significantly shortened when compared with littermates. Mechanistically, we found that chronic HF in Rmp-deficient mice was associated with impaired mitochondrial structure and function, which may be mediated via a transforming growth factor-β/Smad3-proliferator-activated receptor coactivator1α (PGC1α)-dependent mechanism. PGC1α overexpression partially rescued chronic HF in cardiomyocyte-specific Rmp-deficient mice, and Smad3 blockade protected against the loss of PGC1α and adenosine triphosphate content that was induced by silencing RMP in vitro.ConclusionsRMP plays a protective role in chronic HF. RMP may protect cardiomyocytes from injury by maintaining PGC1α-dependent mitochondrial biogenesis and function. The results from this study suggest that RMP may be a potential therapeutic agent for treating HF.

scholarly journals Npa3/ Sc Gpn1 carboxy-terminal tail is dispensable for cell viability and RNA polymerase II nuclear targeting but critical for microtubule stability and function

2017 ◽  
Vol 1864 (3) ◽  
pp. 451-462 ◽  
Author(s):  
Gehenna Guerrero-Serrano ◽  
Leonardo Castanedo ◽  
Gema R. Cristóbal-Mondragón ◽  
Javier Montalvo-Arredondo ◽  
Lina Riego-Ruíz ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Cell Viability ◽  
Rna Polymerase Ii ◽  
Nuclear Targeting ◽  
Microtubule Stability ◽  
Carboxy Terminal ◽  
And Function

scholarly journals Structure and function of the initially transcribing RNA polymerase II–TFIIB complex

Nature ◽  
2012 ◽  
Vol 493 (7432) ◽  
pp. 437-440 ◽  
Author(s):  
Sarah Sainsbury ◽  
Jürgen Niesser ◽  
Patrick Cramer
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Structure And Function ◽  
And Function

scholarly journals Expression, crystallization and preliminary X-ray crystallographic analysis of DNA-directed RNA polymerase subunit L fromThermococcus onnurineusNA1

2014 ◽  
Vol 70 (5) ◽  
pp. 639-642
Author(s):  
Thien-Hoang Ho ◽  
Myoung-Ki Hong ◽  
Ho-Phuong-Thuy Ngo ◽  
Lin-Woo Kang
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Crystallographic Analysis ◽  
Diffusion Method ◽  
Multiprotein Complex ◽  
Hanging Drop ◽  
Gene Encoding ◽  
X Ray ◽  
Cell Parameters ◽  
And Function

RNA polymerase (RNAP) plays a crucial role in gene expression in all organisms. It is a multiprotein complex that produces primary transcript RNA. Generally, the basal transcription apparatus in archaea is simpler than the eukaryotic RNA polymerase II counterpart. To understand the structure and function of archaeal RNAP, theTON-0309gene encoding DNA-directed RNA polymerase subunit L (ToRNAP_L) fromThermococcus onnurineusNA1 was cloned and the protein was overexpressed inEscherichia coli, purified and crystallized. The purified protein was crystallized using the hanging-drop vapour-diffusion method and the crystal diffracted to 2.10 Å resolution. The crystal belonged to the hexagonal space groupP6122, with unit-cell parametersa=b= 42.3,c= 211.2 Å. One molecule was present in the asymmetric unit, with a correspondingVMof 2.5 Å3 Da−1and a solvent content of 50.0%.

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