scholarly journals Recruitment of the protein phosphatase-1 catalytic subunit to promoters by the dual-function transcription factor RFX1

2018 ◽  
Author(s):  
Yoav Lubelsky ◽  
Yosef Shaul
Keyword(s):  
Transcription Factor ◽  
Transcription Factors ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Protein Phosphatase ◽  
Target Genes ◽  
Dna Binding Proteins ◽  
Protein Phosphatase 1 ◽  
Dual Function ◽  
Repression Domain

SummeryRFX proteins are a family of conserved DNA binding proteins involved in various, essential cellular and developmental processes. RFX1 is a ubiquitously expressed, dual-activity transcription factor capable of both activation and repression of target genes.The exact mechanism by which RFX1 regulates its target is not known yet. In this work, we show that the C-terminal repression domain of RFX1 interacts with the Serine/Threonine protein phosphatase PP1c, and that interaction with RFX1 can target PP1c to specific sites in the genome. Given that PP1c was shown to de-phosphorylate several transcription factors, as well as the regulatory C-terminal domain of RNA Polymerase II the recruitment of PP1c to promoters may be a mechanism by which RFX1 regulates the target genes.

Interaction of the TFIIB zinc ribbon with RNA polymerase II

2008 ◽  
Vol 36 (4) ◽  
pp. 595-598 ◽  
Author(s):  
Laura M. Elsby ◽  
Stefan G.E. Roberts
Keyword(s):  
Transcription Factor ◽  
Transcription Factors ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Structural Models ◽  
Initiation Complex ◽  
General Transcription Factors ◽  
Transcription Factor Iib ◽  
General Transcription Factor ◽  
Zinc Ribbon

Transcription by RNA polymerase II requires the assembly of the general transcription factors at the promoter to form a pre-initiation complex. The general transcription factor TF (transcription factor) IIB plays a central role in the assembly of the pre-initiation complex, providing a bridge between promoter-bound TFIID and RNA polymerase II/TFIIF. We have characterized a series of TFIIB mutants in their ability to support transcription and recruit RNA polymerase II to the promoter. Our analyses identify several residues within the TFIIB zinc ribbon that are required for RNA polymerase II assembly. Using the structural models of TFIIB, we describe the interface between the TFIIB zinc ribbon region and RNA polymerase II.

Analysis of transcription factors binding to the human 7SL RNA gene promoter

1999 ◽  
Vol 77 (5) ◽  
pp. 431-438 ◽  
Author(s):  
Jürgen Müller ◽  
Bernd-Joachim Benecke
Keyword(s):  
Transcription Factor ◽  
Transcription Factors ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Rna Polymerase Iii ◽  
Gene Promoter ◽  
7Sl Rna ◽  
Polymerase Iii ◽  
Responsive Element

Transcription of the human 7SL RNA gene by RNA polymerase III depends on the concerted action of transcription factors binding to the gene-internal and gene-external parts of its promoter. Here, we investigated which transcription factors interact with the human 7SL RNA gene promoter and which are required for transcription of the human 7SL RNA gene. A-box/B-box elements were previously identified in 5S RNA, tRNA, and virus associated RNA genes and are recognized by transcription factor IIIC (TFIIIC). The gene-internal promoter region of the human 7SL RNA gene shows only limited similarity to those elements. Nevertheless, competition experiments and the use of highly enriched factor preparations demonstrate that TFIIIC is required for human 7SL transcription. The gene-external part of the promoter includes an authentic cAMP-responsive element previously identified in various RNA polymerase II promoters. Here we demonstrate that members of the activating transcription factor/cyclic AMP-responsive element binding protein (ATF/CREB) transcription factor family bind specifically to this element in vitro. However, the human 7SL RNA gene is not regulated by cAMP in vivo. Furthermore, in vitro transcription of the gene does not depend on ATF/CREB transcription factors. It rather appears that a transcription factor with DNA-binding characteristics like ATF/CREB proteins but otherwise different properties is required for human 7SL RNA transcription.Key words: 7SL RNA, ATF, CRE, TFIIIC, RNA polymerase III.

scholarly journals DAF-16/FOXO requires Protein Phosphatase 4 to initiate transcription of stress resistance and longevity promoting genes

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Ilke Sen ◽  
Xin Zhou ◽  
Alexey Chernobrovkin ◽  
Nataly Puerta-Cavanzo ◽  
Takaharu Kanno ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Rna Polymerase Ii ◽  
Stress Resistance ◽  
Protein Phosphatase ◽  
Target Genes ◽  
Transcriptional Regulator ◽  
Specific Protein ◽  
Transcriptional Initiation ◽  
C Elegans ◽  
Rate Limiting

AbstractIn C. elegans, the conserved transcription factor DAF-16/FOXO is a powerful aging regulator, relaying dire conditions into expression of stress resistance and longevity promoting genes. For some of these functions, including low insulin/IGF signaling (IIS), DAF-16 depends on the protein SMK-1/SMEK, but how SMK-1 exerts this role has remained unknown. We show that SMK-1 functions as part of a specific Protein Phosphatase 4 complex (PP4SMK-1). Loss of PP4SMK-1 hinders transcriptional initiation at several DAF-16-activated genes, predominantly by impairing RNA polymerase II recruitment to their promoters. Search for the relevant substrate of PP4SMK-1 by phosphoproteomics identified the conserved transcriptional regulator SPT-5/SUPT5H, whose knockdown phenocopies the loss of PP4SMK-1. Phosphoregulation of SPT-5 is known to control transcriptional events such as elongation and termination. Here we also show that transcription initiating events are influenced by the phosphorylation status of SPT-5, particularly at DAF-16 target genes where transcriptional initiation appears rate limiting, rendering PP4SMK-1 crucial for many of DAF-16’s physiological roles.

scholarly journals Mass spectrometry and biochemical analysis of RNA polymerase II: targeting by protein phosphatase-1

2010 ◽  
Vol 347 (1-2) ◽  
pp. 79-87 ◽  
Author(s):  
Marina Jerebtsova ◽  
Sergei A. Klotchenko ◽  
Tatiana O. Artamonova ◽  
Tatiana Ammosova ◽  
Kareem Washington ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Protein Phosphatase ◽  
Biochemical Analysis ◽  
Protein Phosphatase 1

scholarly journals Expression analysis of transcription factors in sugarcane during cold stress

2023 ◽  
Vol 83 ◽  
Author(s):  
S. U. Rehman ◽  
K. Muhammad ◽  
E. Novaes ◽  
Y. Que ◽  
A. Din ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Transcription Factors ◽  
Rna Polymerase ◽  
Cold Stress ◽  
Rna Polymerase Ii ◽  
Rna Polymerase Iii ◽  
Regulatory Region ◽  
Transcription Factor Activity ◽  
Factor Activity ◽  
Upregulated Genes

Abstract Transcription factors (TF) are a wide class of genes in plants, and these can regulate the expression of other genes in response to various environmental stresses (biotic and abiotic). In the current study, transcription factor activity in sugarcane was examined during cold stress. Initially, RNA transcript reads of two sugarcane cultivars (ROC22 and GT08-1108) under cold stress were downloaded from SRA NCBI database. The reads were aligned into a reference genome and the differential expression analyses were performed with the R/Bioconductor edgeR package. Based on our analyses in the ROC22 cultivar, 963 TF genes were significantly upregulated under cold stress among a total of 5649 upregulated genes, while 293 TF genes were downregulated among a total of 3,289 downregulated genes. In the GT08-1108 cultivar, 974 TF genes were identified among 5,649 upregulated genes and 283 TF genes were found among 3,289 downregulated genes. Most transcription factors were annotated with GO categories related to protein binding, transcription factor binding, DNA-sequence-specific binding, transcription factor complex, transcription factor activity in RNA polymerase II, the activity of nucleic acid binding transcription factor, transcription corepressor activity, sequence-specific regulatory region, the activity of transcription factor of RNA polymerase II, transcription factor cofactor activity, transcription factor activity from plastid promoter, transcription factor activity from RNA polymerase I promoter, polymerase II and RNA polymerase III. The findings of above results will help to identify differentially expressed transcription factors during cold stress. It also provides a comprehensive analysis of the regulation of the transcription activity of many genes. Therefore, this study provides the molecular basis for improving cold tolerance in sugarcane and other economically important grasses.

scholarly journals Protein Phosphatase-1 Dephosphorylates the C-terminal Domain of RNA Polymerase-II

2002 ◽  
Vol 277 (43) ◽  
pp. 40442-40448 ◽  
Author(s):  
Kareem Washington ◽  
Tatyana Ammosova ◽  
Monique Beullens ◽  
Marina Jerebtsova ◽  
Ajit Kumar ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Protein Phosphatase ◽  
Protein Phosphatase 1 ◽  
Terminal Domain

scholarly journals Nuclear Targeting of Protein Phosphatase-1 by HIV-1 Tat Protein

2005 ◽  
Vol 280 (43) ◽  
pp. 36364-36371 ◽  
Author(s):  
Tatyana Ammosova ◽  
Marina Jerebtsova ◽  
Monique Beullens ◽  
Bart Lesage ◽  
Angela Jackson ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Protein Phosphatase ◽  
Protein Phosphatase 1 ◽  
Tat Protein ◽  
Nuclear Targeting ◽  
Cyclin T1 ◽  
Immunodeficiency Virus ◽  
Hiv 1

Transcription of human immunodeficiency virus (HIV)-1 genes is activated by HIV-1 Tat protein, which induces phosphorylation of the C-terminal domain of RNA polymerase-II by CDK9/cyclin T1. We previously showed that Tat-induced HIV-1 transcription is regulated by protein phosphatase-1 (PP1). In the present study we demonstrate that Tat interacts with PP1 and that disruption of this interaction prevents induction of HIV-1 transcription. We show that PP1 interacts with Tat in part through the binding of Val36 and Phe38 of Tat to PP1 and that Tat is involved in the nuclear and subnuclear targeting of PP1. The PP1 binding mutant Tat-V36A/F38A displayed a decreased affinity for PP1 and was a poor activator of HIV-1 transcription. Surprisingly, Tat-Q35R mutant that had a higher affinity for PP1 was also a poor activator of HIV-1 transcription, because strong PP1 binding competed out binding of Tat to CDK9/cyclin T1. Our results suggest that Tat might function as a nuclear regulator of PP1 and that interaction of Tat with PP1 is critical for activation of HIV-1 transcription by Tat.

scholarly journals Acetyl Coenzyme A Stimulates RNA Polymerase II Transcription and Promoter Binding by Transcription Factor IID in the Absence of Histones

2000 ◽  
Vol 20 (6) ◽  
pp. 1923-1930 ◽  
Author(s):  
Shelly K. Galasinski ◽  
Tricia N. Lively ◽  
Alexandra Grebe de Barron ◽  
James A. Goodrich
Keyword(s):  
Transcription Factor ◽  
Transcription Factors ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Coenzyme A ◽  
Dnase I ◽  
Acetyl Coa ◽  
Acetyl Coenzyme A ◽  
Dnase I Footprinting ◽  
Rna Polymerase Ii Transcription

ABSTRACT Protein acetylation has emerged as a means of controlling levels of mRNA synthesis in eukaryotic cells. Here we report that acetyl coenzyme A (acetyl-CoA) stimulates RNA polymerase II transcription in vitro in the absence of histones. The effect of acetyl-CoA on basal and activated transcription was studied in a human RNA polymerase II transcription system reconstituted from recombinant and highly purified transcription factors. Both basal and activated transcription were stimulated by the addition of acetyl-CoA to transcription reaction mixtures. By varying the concentrations of general transcription factors in the reaction mixtures, we found that acetyl-CoA decreased the concentration of TFIID required to observe transcription. Electrophoretic mobility shift assays and DNase I footprinting revealed that acetyl-CoA increased the affinity of the general transcription factor TFIID for promoter DNA in a TBP-associated factor (TAF)-dependent manner. Interestingly, acetyl-CoA also caused a conformational change in the TFIID-TFIIA-promoter complex as assessed by DNase I footprinting. These results show that acetyl-CoA alters the DNA binding activity of TFIID and indicate that this biologically important cofactor functions at multiple levels to control gene expression.

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