Any process involved in the assembly of the RNA polymerase I preinitiation complex (PIC) at an RNA polymerase I promoter region of a DNA template, resulting in the subsequent synthesis of RNA from that promoter. The initiation phase includes PIC assembly …
Antibodies for proteins involved in negative regulation of transcription elongation from RNA polymerase I promoter pathways, according to their Panther/Gene Ontology Classification
Rabbit antibodies to RNA polymerase I from a rat hepatoma have been used to localize the enzyme in a variety of cells at the light and electron microscopic level. In interphase cells the immunofluorescence pattern indicated that polymerase I is contained exclusively within the nucleolus. That this fluorescence, which appeared punctated rather than uniform, represented transcriptional complexes of RNA polymerase I and rRNA genes was suggested by the observation that it was enhanced in regenerating liver and in a hepatoma and was markedly diminished in cells treated with actinomycin D. Electron microscopic immunolocalization using gold-coupled second antibodies showed that transcribed rRNA genes are located in, and probably confined to, the fibrillar centers of the nucleolus. In contrast, the surrounding dense fibrillar component, previously thought to be the site of nascent pre-rRNA, did not contain detectable amounts of polymerase I. During mitosis, polymerase I molecules were detected by ...
The pharmacologic inhibition of RNA Pol I is becoming a potentially important therapeutic strategy in cancer (7, 19, 23). The therapeutic index using Pol I inhibition relies at least in part on the fact that tumor cells are often found to be in an anabolic state, with higher levels of ribosome biosynthesis than their corresponding normal counterparts (7, 9, 43). A validated assay that can determine whether there is indeed an increase in Pol I activity in routinely obtained tissue specimens, as well as a similarly applicable pharmacodynamic marker of target inhibition, would be a valuable companion diagnostic for such therapeutic trials.. We developed a CISH assay to examine the level of expression of the 5′ETS/45S rRNA gene in routinely processed human clinical tissue FFPE specimens. In contrast to the highly stable 18S/28S rRNA, the 5′ETS region is processed cotranscriptionally and is short-lived, and hence well suited for use as a marker for Pol I transcription activity (17). As of now, we ...
Complete information for RRN3 gene (Protein Coding), RRN3 Homolog, RNA Polymerase I Transcription Factor, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
A cyclic AMP-dependent nuclear protein kinase was found to be closely associated with rat liver nucleolar RNA polymerase I throughout most of its purification. This protein kinase was purified to near homogeneity. It exhibits a number of unusual catalytic properties, including the inability to utilize Mn2+ when RNA polymerase is the substrate and the ability to phosphorylate both acidic and basic substrates. Phosphorylation of RNA polymerase I by this protein kinase results in the formation of phosphoester bonds characteristic of phosphoserine and phosphothreonine. Radioautography of polyacrylamide-gel electrophoretograms of the phosphorylated RNA polymerase I revealed that the 32P was located primarily on enzyme subunits SA1, SA3, SA5, and SA6 [nomenclature of Kedinger, Gissinger & Chambon (1974) Eur. J. Biochem, 44, 421-436]. ...
FIG. 3. DRB Dreferentiallv - 5 , 6 = Dichloro - 1 - # ? - D - ribofuranosylbenzimidazole Inhibits Transcription Elongation by RNA Polymerase I 1 in Vitro
Monoallelic expression within a gene family is found in pathogens exhibiting antigenic variation and in mammalian olfactory neurons. Trypanosoma brucei, a lethal parasite living in the human bloodstream, expresses variant surface glycoprotein (VSG) from 1 of 15 bloodstream expression sites (BESs) by virtue of a multifunctional RNA polymerase I. The active BES is transcribed in an extranucleolar compartment termed the expression site body (ESB), whereas silent BESs, located elsewhere within the nucleus, are repressed epigenetically. The regulatory mechanisms, however, are poorly understood. Here we show that two essential subunits of the basal class I transcription factor A (CITFA) predominantly occupied the promoter of the active BES relative to that of a silent BES, a phenotype that was maintained after switching BESs in situ. In these experiments, high promoter occupancy of CITFA was coupled to high levels of both promoter-proximal RNA abundance and RNA polymerase I occupancy. Accordingly, ...
Given its unique ability to regulate RNA polymerase I activity and synthesis of rRNA, we investigated the role of the transcription factor TIF-IA in the developing and adult nervous system. We demonstrate that TIF-IA-dependent functions are essential for the survival of both neural progenitors and nondividing neurons of the adult hippocampus. TIF-IA ablation in proliferating cells leads rapidly to activation of the apoptotic machinery. In contrast, in adult hippocampal neurons, significant signs of neurodegeneration are evident only several months after inducing the mutation, although strong interference with pre-rRNA synthesis occurs already early after induction of the mutation.. Increased levels of the p53 protein are found after TIF-IA ablation in rapidly dividing cells as well as in postmitotic neurons. The precise mechanism by which loss of TIF-IA leads to p53 increase requires further investigation. In neural progenitors one possible mechanism regulating p53 protein levels upon TIF-IA ...
Inhibition of Pol I Transcription Treats Murine and Human AML by Targeting the Leukemia-Initiating Cell Population Investigators revealed that the selective inhibitor of RNA polymerase I (Pol I) transcription, CX-5461, effectively treats aggressive acute myeloid leukemia (AML), including MLL-driven AML, and outperforms standard chemotherapies. In addition to the previously characterized mechanism of action of CX-5461, the induction of p53-dependant apoptotic cell death, inhibition of Pol I transcription also demonstrated potent efficacy in p53null AML in vivo. [Blood] Abstract Pre‐Clinical Validation of a Selective Anti‐Cancer Stem Cell Therapy for Numb‐Deficient Human Breast Cancers Using patient‐derived xenografts, researchers showed that expansion of the cancer stem cell (CSC) pool, due to altered self‐renewing divisions, is also a feature of Numb‐deficient human breast cancers. In these cancers, using the inhibitor Nutlin‐3 to restore p53, they corrected the defective ...
Splicing factors, usually associated with RNA polymerase II transcripts, have a temporary home near sites of RNA polymerase I transcription, as shown on page 51 by Bubulya et al.. During interphase, premRNA splicing factors such as the serine arginine-rich (SR) proteins reside in nuclear speckles, along with other pre-mRNA processing proteins. The speckles disassemble during mitosis, and then reform in G1. By viewing speckle reformation, the group finds that SR proteins first make a side trip and gather in nucleolar organizing region-associated patches (NAPs), around areas where rDNA is transcribed.. Inhibiting mRNA transcription prolonged the life of NAPs and also caused SR proteins to accumulate near nucleoli in interphase cells. Without their pre-mRNA transcript targets available, SR protein traffic was backed up at a location it would otherwise move through rapidly.. NAPs contained hypophosphorylated SR proteins, which may self-associate and thus accumulate in patches. NAPs also contained an ...
The Saccharomyces Genome Database (SGD) provides comprehensive integrated biological information for the budding yeast Saccharomyces cerevisiae.
ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. Regulates polymerase II transcription. Also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. Regulates negatively DNA replication. Not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome. Is also associated with histone deacetylase (HDAC) activity (By similarity). Required for the bridging of SNF2, the FACT complex, the PAF complex as well as the U2 snRNP complex to H3K4me3. Functions to modulate the efficiency of pre-mRNA splicing in part through physical bridging of spliceosomal components to H3K4me3. Required for maintaining open chromatin and pluripotency in embryonic stem cells ...
Reb1 of Schizosaccharomyces pombe represents a family of multifunctional proteins that bind to specific terminator sites (Ter) and cause polar termination of transcription catalyzed by RNA polymerase I (pol I) and arrest of replication forks approaching the Ter sites from the opposite direction. However, it remains to be investigated whether the same mechanism causes arrest of both DNA transactions. Here, we present the structure of Reb1 as a complex with a Ter site at a resolution of 2.7 Å. Structure-guided molecular genetic analyses revealed that it has distinct and well-defined DNA binding and transcription termination (TTD) domains. The region of the protein involved in replication termination is distinct from the TTD. Mechanistically, the data support the conclusion that transcription termination is not caused by just high affinity Reb1-Ter protein-DNA interactions. Rather, protein-protein interactions between the TTD with the Rpa12 subunit of RNA pol I seem to be an integral part of the ...
Complete information for UBTF gene (Protein Coding), Upstream Binding Transcription Factor, RNA Polymerase I, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
This study uses structural, proteomic and functional approaches to elucidate how the translational repressor LSM14 interfaces with a number of mRNA silencing factors, including 4E‐T, DDX6 and EDC4. Structures of LSM14‐4E‐T and LSM14‐DDX6 complexes highlight the role of short linear interacting motifs (SLiMs) in organizing multiprotein complexes in mRNA metabolism.. ...
Hung, S, Lesmana, A, Peck, A et al 2017, Cell cycle and growth stimuli regulate different steps of RNA polymerase I transcription, Gene, vol. 612, pp. 36-48. ...
The problems appear to be with my probes because the control actin probe which comes with the Strip-EZ DNA kit works perfectly and I get a beautiful signal within 30 minutes!! To get my own probes, I make cDNA from mouse RNA and then PCR up my region of interest using the cDNA as a template. I get great PCR bands. I then phenol:chlroform clean my probes and label with 32-P using Ambion Strip-EZ DNA kit. When I check the incorporation, it is not great but is workable (around 50-60%). I run a blot of mouse RNA usually not going above 10ug. I use standard wash conditions and the same ones that I used for the control.....but NOTHING ...
casSAR Dugability of D3ZYB7 | Taf1b | TATA box-binding protein-associated factor RNA polymerase I subunit B - Also known as TAF1B_RAT, Taf1b. Component of RNA polymerase I core factor complex that acts as a GTF2B/TFIIB-like factor and plays a key role in multiple steps during transcription initiation such as pre-initiation complex (PIC) assembly and postpolymerase recruitment events in polymerase I (Pol I) transcription. Binds rDNA promoters and plays a role in Pol I recruitment as a component of the SL1/TIF-IB complex and, possibly, directly through its interaction with RRN3 (By similarity). Interacts with FLNA (via N-terminus) (By similarity). Component of the transcription factor SL1/TIF-IB complex, composed of TBP and at least TAF1A, TAF1B, TAF1C and TAF1D. In the complex interacts directly with TBP, TAF1A and TAF1C. Interaction of the SL1/TIF-IB subunits with TBP excludes interaction of TBP with the transcription factor IID (TFIID) subunits. Interacts with TBP and RRN3 (By similarity).
Structures of RNA polymerase I transcription machinery revealed a ratcheting motion within the complex in coordination with three distinct functional states, implicating a novel mechanism for promoter bubble opening in the absence of ATP hydrolysis.
Required for efficient transcription initiation by RNA polymerase I. Required for the formation of the competent preinitiation complex (PIC). Dissociates from pol I as a consequence of transcription. In vitro, cannot activate transcription in a subsequent transcription reaction (By similarity ...
Gene duplication and exonization of intronic transposed elements are two mechanisms that enhance genomic diversity. We examined whether there is less selection against exonization of transposed elements in duplicated genes than in single-copy genes. Genome-wide analysis of exonization of transposed elements revealed a higher rate of exonization within duplicated genes relative to single-copy genes. The gene for TIF-IA, an RNA polymerase I transcription initiation factor, underwent a humanoid-specific triplication, all three copies of the gene are active transcriptionally, although only one copy retains the ability to generate the TIF-IA protein. Prior to TIF-IA triplication, an Alu element was inserted into the first intron. In one of the non-protein coding copies, this Alu is exonized. We identified a single point mutation leading to exonization in one of the gene duplicates. When this mutation was introduced into the TIF-IA coding copy, exonization was activated and the level of the protein-coding
Taf1d (untagged) - Mouse TATA box binding protein (Tbp)-associated factor, RNA polymerase I, D (Taf1d), transcript variant 2, (10ug), 10 µg.
This gene encodes a transcription termination factor that is localized to the nucleolus and plays a critical role in ribosomal gene transcription. The encoded protein mediates the termination of RNA polymerase I transcription by binding to Sal box terminator elements downstream of pre-rRNA coding regions. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. This gene shares the symbol/alias TFF1 with another gene, NK2 homeobox 1, also known as thyroid transcription factor 1, which plays a role in the regulation of thyroid-specific gene expression ...
The present study clearly demonstrates that DOX-induced acute cardiac toxicity was significantly exacerbated in Mrp1−/− mice. Whereas morphometric analysis of electron micrographs of the heart showed significant damage to the mitochondria and the cytoplasm after DOX treatment, consistent with previous findings (Yen et al., 1996), this injury was not different in the two genotypes. In contrast, the nucleus showed significantly more damage after DOX treatment of Mrp1−/− mice, with fragmentation of the nucleolus, segregation of granular and fibrillar components, and condensation of nucleoli with compacted chromatin. The nucleolus is the primary site of transcription, assembly, and processing of cellular RNA (Antoniali et al., 2014), with a tripartite organization that reflects the different steps of ribosomal biogenesis. RNA polymerase I transcription starts in the fibrillar center, with the dense fibrillary component the site of initial stages of pre-rRNA processing and a granular ...
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
Rabbit anti-RNA Polymerase II, Phospho (S5) Antibody, Affinity Purified - 100 µl (10 blots) - Bethyl Laboratories, Inc. - antibodies
This study has 2 phases. Each phase will last 10 weeks and there will be a 4-week break between the 2 phases. Thus, you will be enrolled in the study for a total of 24 weeks. Over the course of the 24-week period we will schedule to see you in-person 6 times and check-in with you on the telephone 4 times, 2 times during each phase.. Phase I. Screening (may be the same day as the baseline visit) - Research personnel will determine if you are eligible to participate in this study.. Visit 1 - Baseline Visit, Start Study Medication. Phone Call 1 - Check in to see how you are feeling after starting the study medication. Visit 2 - 4 Weeks after Baseline, Increase Study Medication if tolerated. Phone Call 2 - Check in to see how you are feeling after increasing the study medication. Visit 3/ Phase I Termination Visit - 10 Weeks after Baseline (Phase I Termination Visit). 4 Week Break (no study medication). Phase II. Visit 4/ Phase II Baseline - 14 Weeks after Baseline, Start Study Medication. Phone ...
This study has 2 phases. Each phase will last 10 weeks and there will be a 4-week break between the 2 phases. Thus, you will be enrolled in the study for a total of 24 weeks. Over the course of the 24-week period we will schedule to see you in-person 6 times and check-in with you on the telephone 4 times, 2 times during each phase.. Phase I. Screening (may be the same day as the baseline visit) - Research personnel will determine if you are eligible to participate in this study.. Visit 1 - Baseline Visit, Start Study Medication. Phone Call 1 - Check in to see how you are feeling after starting the study medication. Visit 2 - 4 Weeks after Baseline, Increase Study Medication if tolerated. Phone Call 2 - Check in to see how you are feeling after increasing the study medication. Visit 3/ Phase I Termination Visit - 10 Weeks after Baseline (Phase I Termination Visit). 4 Week Break (no study medication). Phase II. Visit 4/ Phase II Baseline - 14 Weeks after Baseline, Start Study Medication. Phone ...
Taf1a - Taf1a (untagged ORF) - Rat TATA box binding protein (Tbp)-associated factor, RNA polymerase I, A (Taf1a), (10 ug) available for purchase from OriGene - Your Gene Company.
Reagents for the antigen UBP1 / upstream binding protein 1 (LBP-1a) stained with Streptavidin / Avidin in the Antibody Database
Custom Services: If you are interested in Northern blot constructed with any mouse RNA tissue of any strain or required blots to be specifically prepared to meet your application, our custom service scientists can make it for you. C For more information, contact technical support at [email protected] or at 858 546 0720.lick here for more information or contact our technical service representative at [email protected] or at 858 546 0720. ...
Transcription termination factor 1 is a protein that in humans is encoded by the TTF1 gene. GRCh38: Ensembl release 89: ENSG00000125482 - Ensembl, May 2017 "Human PubMed Reference:". Evers R, Grummt I (Aug 1995). "Molecular coevolution of mammalian ribosomal gene terminator sequences and the transcription termination factor TTF-I". Proc Natl Acad Sci U S A. 92 (13): 5827-31. doi:10.1073/pnas.92.13.5827. PMC 41594 . PMID 7597036. "Entrez Gene: TTF1 transcription termination factor, RNA polymerase I". Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1-2): 171-4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791-806. doi:10.1101/gr.6.9.791. PMID 8889548. Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full ...
Confocal microscopy and in situ hybridization procedures have led to enormous progress in the visualization of the spatial organization and dynamics of transcription and RNA‐processing machinery in eukaryotic cells. It is well established that the nucleus is a highly organized structure composed of many different territories, subdomains and organelles (Lamond and Earnshaw, 1998). A state‐of‐the‐art account of the nuclear architecture of plant cells was given by P.Shaw (John Innes Centre, Norwich, UK). Mapping of the RNA polymerase I transcription and rRNA processing sites, using different pre‐rRNA, snoRNA and nucleolar protein probes, indicates that the plant cell nucleolus is organized as a series of concentric layers in which transcription and successive rRNA processing reactions occur. As in vertebrate cells, plant cells contain coiled bodies (CBs), nuclear organelles of still poorly defined function. Since CB components include several small RNAs, and also proteins related to ...
Most prokaryotes and archaeans use the same RNA polymerase to transcribe mRNA and functional non-coding RNAs (e.g. ribosomal RNAs or transfer RNAs). Whereas eukaryotes (organisms in which the genetic material is contained within a nucleus) use specialized RNAPs, each responsible for transcribing different classes of RNA. RNA polymerase II (abbreviated RNAP II or RNA Pol II), is the enzyme responsible for transcribing the vast majority of protein-coding genes in eukaryotes. It is also responsible for transcribing the majority of genes encoding short nuclear RNAs (snRNAs) and micro RNAs (miRNAs). As such, RNAP II is the most well-studied and well understood of the eukaryotic RNAPs. Genes transcribed by RNAP II are referred to as "type II genes" and comprise the vast majority of genes present in eukaryotic genomes. RNA polymerase I (RNAP I or RNA Pol I) transcribes most of the ribosomal RNAs in a eukaryotic cell. RNA polymerase III (RNAP III or RNA pol III) transcribes the tRNA precursors, as well ...
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively.
Link to Pubmed [PMID] - 17270230. Virology 2007 Jun;362(2):271-82. The transcription/replication activity of ribonucleoproteins derived from influenza A primary isolates of human (A/Paris/908/97) or avian origin (A/Mallard/Marquenterre/MZ237/83, A/Hong Kong/156/97) was compared upon reconstitution in mammalian or avian cells, using viral-like reporter RNAs synthesized under the control of the human and chicken RNA polymerase I promoters, respectively. In avian cells, transcription/replication activities were in the same range with all ribonucleoproteins tested. In human cells, ribonucleoproteins derived from A/Mallard/Marquenterre/MZ237/83 showed reduced transcription/replication activity and reduced NP binding to the PB1-PB2-PA complex (P) or to the isolated PB2 subunit, as compared to the ribonucleoproteins derived from A/Paris/908/97. Both defects were restored when PB2 residue Glu-627 was changed to a Lys. Ribonucleoproteins derived from the human A/Hong Kong/156/97 H5N1 isolate showed ...
In the present study, we have shown that the PNC actively incorporates Br-UTP and FITC-CTP in a transcription assay using permeabilized cells. Many studies have used this assay to investigate transcription patterns in the cell nucleus (Hozak et al., 1994; Aoki et al., 1997; Fay et al., 1997; Neugebauer and Roth, 1997) since its initial establishment (Jackson et al., 1993; Wansink et al., 1993). Our observation that the PNC actively incorporates labeled nucleotides in a DNA-dependent manner after 5 min of pulse labeling suggests that the PNC is a site of transcription. Inhibition of RNA polymerase I either by addition of actinomycin D in the transcription cocktail or by pretreatment of cells with cycloheximide does not affect the Br-UTP incorporation, indicating that transcription of nascent RNA in the PNC is unlikely to involve RNA polymerase I. This finding is consistent with the report by Matera et al. (1995) that 28S rRNA was not detected in the PNC using in situ hybridization and our ...
JOSD3, OACA2, OACA3, SNORA32, TATA box-binding protein-associated factor RNA polymerase I subunit D,Josephin domain containing 3,TATA box binding protein (TBP)-associated factor, RNA polymerase I, D, 41kDa,small nucleolar RNA, H/ACA box ...
Deregulation of translational control can promote cellular transformation. Protein synthesis and the expression of components of the translation machinery are elevated in cancers and contribute to tumorigenesis (1-5, 7). Here, we show that nuclear ErbB2 promotes binding of RNA Pol I to rDNA, co-occupies the rRNA gene with β-actin and RNA Pol I, and stimulates rRNA production and protein translation independently of traditional ErbB2 downstream PI3-K and ERK signalings, suggesting that nuclear ErbB2 may contribute to oncogenesis by upregulating total cellular translation. rRNA synthesis by RNA Pol I plays a critical role in production of mature ribosomes that are central protein synthesis machinery of the cells. Perturbation of RNA Pol I activity as well as rRNA and protein biosynthesis (i.e., translation control) by oncoproteins such as Myc or tumor suppressors p53, RB, and ADP ribosylation factor has been reported to be associated with tumor development (1, 2, 7-10). The capability of Myc to ...
CX-5461 is a first-in-class non-genotoxic small molecule targeted inhibitor of RNA polymerase I (Pol I) that activates the p53 pathway without causing DNA damage. CX-5461 selectively inhibits rRNA synthesis by Pol I in the nucleolus, but does not inhibit mRNA synthesis by RNA Polymerase II (Pol II) and does not inhibit DNA replication or protein synthesis. Inhibition of Pol I results in nucleolar stress and release of ribosomal proteins (RP) from the nucleolus. The RP bind to Mdm2 and liberate p53 to orchestrate apoptosis in cancer cells. CX-5461 demonstrates a favorable preclinical profile, potently and selectively kills cancer cells, demonstrates robust in vivo efficacy in multiple models, and has demonstrated oral bioavailability in multiple species.
RNA polymerase sigma 70 antibody [2G10] for ELISA, IP, WB, Functional Assay. Anti-RNA polymerase sigma 70 mAb (GTX12088) is tested in Bacteria samples. 100% Ab-Assurance.
TY - JOUR. T1 - Reassessment of the in vivo functions of DNA polymerase I and RNase H in bacterial cell growth. AU - Fukushima, Sanae. AU - Itaya, Mitsuhiro. AU - Kato, Hiroaki. AU - Ogasawara, Naotake. AU - Yoshikawa, Hirofumi. PY - 2007/12/1. Y1 - 2007/12/1. N2 - A major factor in removing RNA primers during the processing of Okazaki fragments is DNA polymerase I (Pol I). Pol I is thought to remove the RNA primers and to fill the resulting gaps simultaneously. RNase H, encoded by rnh genes, is another factor in removing the RNA primers, and there is disagreement with respect to the essentiality of both the polA and rnh genes. In a previous study, we looked for the synthetic lethality of paralogs in Bacillus subtilis and detected several essential doublet paralogs, including the polA ypcP pair. YpcP consists of only the 5′-3′ exonuclease domain. In the current study, we first confirmed that the polA genes of both Escherichia coli and B. subtilis could be completely deleted. We found that ...
Inquiry (23534) for Abcams Anti-RNA polymerase II CTD repeat YSPTSPS (phospho S5) antibody [4H8] - ChIP Grade. Our in-house scientific support team are here to help you with any technical questions or queries
This ${affineX}. Is licensed under a Creative Commons ${SC-} License. In addition to the (SLA) licenses including the enhanced (UBMTA) and the release that forms the ease that dosent while mininizing the cost s of publication of this document were not defrayed in part or in whole by the payment of page charges. The document must therefore be hereby marked "non-advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact unless otherwise indicated by authors with competing interest statments found herein. Content for informational and educational use only. All rights reserved. The contents provided here are solely the responsibility of the author and dose not identify or necessarily represent the official views, components of/or by a Science Education Partnership, Awards, or the NIH Research Resources/ Human Health Services. The Administration has offered regulations from the Department of Health and Human Services (Standards for Privacy of Individually Identifiable ...
Rabbit recombinant monoclonal RNA polymerase II CTD repeat YSPTSPS (phospho S1801) antibody [EP1510Y] validated for WB, IP, IHC, ICC/IF and tested in Human…
An investigation of the functional role of the MADS-box γ and MADS-box α type I transcription factors: AGAMOUS-LIKE 28 and AGAMOUS-LIKE 36. ...
View teatox133s blog post, Core Factors In Teatox - An Introduction, on BlackPlanet.com. Worlds largest free African-American online community where Black women and Black men meet to chat, discuss and
Compare Upstream Binding Transcription Factor, RNA Polymerase I-Like 1 ELISA Kits from leading suppliers on Biocompare. View specifications, prices, citations, reviews, and more.
Nuclear myosin 1c (NM1) mediates RNA polymerase I (pol I) transcription activation and cell cycle progression by facilitating PCAF-mediated H3K9 acetylation, but the molecular mechanism by which NM1 is regulated remains unclear. Here, we report that at early G1 the glycogen synthase kinase (GSK) 3β phosphorylates and stabilizes NM1, allowing for NM1 association with the chromatin. Genomic analysis by ChIP-Seq showed that this mechanism occurs on the rDNA as active GSK3β selectively occupies the gene. ChIP assays and transmission electron microscopy in GSK3β-/- mouse embryonic fibroblasts indicated that at G1 rRNA synthesis is suppressed due to decreased H3K9 acetylation leading to a chromatin state incompatible with transcription. We found that GSK3β directly phosphorylates the endogenous NM1 on a single serine residue (Ser-1020) located within the NM1 C-terminus. In G1 this phosphorylation event stabilizes NM1 and prevents NM1 polyubiquitination by the E3 ligase UBR5 and proteasome-mediated ...