scholarly journals Periodic Oxaliplatin Administration in Synergy with PER2‐Mediated PCNA Transcription Repression Promotes Chronochemotherapeutic Efficacy of OSCC

2019 ◽  
Vol 6 (21) ◽  
pp. 1900667 ◽  
Author(s):  
Qingming Tang ◽  
Mengru Xie ◽  
Shaoling Yu ◽  
Xin Zhou ◽  
Yanling Xie ◽  
...  
Keyword(s):  
Transcription Repression

Gene transcription repression inClostridium beijerinckiiusing CRISPR-dCas9

2016 ◽  
Vol 113 (12) ◽  
pp. 2739-2743 ◽  
Author(s):  
Yi Wang ◽  
Zhong-Tian Zhang ◽  
Seung-Oh Seo ◽  
Patrick Lynn ◽  
Ting Lu ◽  
...  
Keyword(s):  
Gene Transcription ◽  
Transcription Repression

scholarly journals Structural basis of RNA polymerase III transcription repression by Maf1

2019 ◽  
Author(s):  
Matthias K. Vorländer ◽  
Florence Baudin ◽  
Robyn D. Moir ◽  
René Wetzel ◽  
Wim J. H. Hagen ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Binding Site ◽  
Transcription Initiation ◽  
Rna Polymerase Iii ◽  
Structural Basis ◽  
Metabolic Efficiency ◽  
Transcription Repression ◽  
Polymerase Iii ◽  
Wide Range ◽  
Pol Iii

ABSTRACTMaf1 is a highly conserved central regulator of transcription by RNA polymerase III (Pol III), and Maf1 activity influences a wide range of phenotypes from metabolic efficiency to lifespan. Here, we present a 3.3 Å cryo-EM structure of yeast Maf1 bound to Pol III, which establishes how Maf1 achieves transcription repression. In the Maf1-bound state, Pol III elements that are involved in transcription initiation are sequestered, and the active site is sealed off due to ordering of the mobile C34 winged helix 2 domain. Specifically, the Maf1 binding site overlaps with the binding site of the Pol III transcription factor TFIIIB and DNA in the pre-initiation complex, rationalizing that binding of Maf1 and TFIIIB to Pol III are mutually exclusive. We validate our structure using variants of Maf1 with impaired transcription-inhibition activity. These results reveal the exact mechanism of Pol III inhibition by Maf1, and rationalize previous biochemical data.

scholarly journals A new model of cell cycle-regulated transcription: repression of the cyclin A promoter by CDF-1 and anti-repression by E2F

Oncogene ◽  
1998 ◽  
Vol 16 (23) ◽  
pp. 2957-2963 ◽  
Author(s):  
Ningshu Liu ◽  
Frances C Lucibello ◽  
Kurt Engeland ◽  
Rolf Müller
Keyword(s):  
Cell Cycle ◽  
Cyclin A ◽  
New Model ◽  
Transcription Repression

scholarly journals Control of the DNA Methylation System Component MBD2 by Protein Arginine Methylation

2006 ◽  
Vol 26 (19) ◽  
pp. 7224-7235 ◽  
Author(s):  
Choon Ping Tan ◽  
Sara Nakielny
Keyword(s):  
Dna Methylation ◽  
Complex Formation ◽  
Histone Deacetylases ◽  
Mammalian Cells ◽  
Genome Stability ◽  
Epigenetic Modification ◽  
Arginine Methylation ◽  
System Component ◽  
Transcription Repression ◽  
Mbd Proteins

ABSTRACT DNA methylation is vital for proper chromatin structure and function in mammalian cells. Genetic removal of the enzymes that catalyze DNA methylation results in defective imprinting, transposon silencing, X chromosome dosage compensation, and genome stability. This epigenetic modification is interpreted by methyl-DNA binding domain (MBD) proteins. MBD proteins respond to methylated DNA by recruiting histone deacetylases (HDAC) and other transcription repression factors to the chromatin. The MBD2 protein is dispensable for animal viability, but it is implicated in the genesis of colon tumors. Here we report that the MBD2 protein is controlled by arginine methylation. We identify the protein arginine methyltransferase enzymes that catalyze this modification and show that arginine methylation inhibits the function of MBD2. Arginine methylation of MBD2 reduces MBD2-methyl-DNA complex formation, reduces MBD2-HDAC repression complex formation, and impairs the transcription repression function of MBD2 in cells. Our report provides a molecular description of a potential regulatory mechanism for an MBD protein family member. It is the first to demonstrate that protein arginine methyltransferases participate in the DNA methylation system of chromatin control.

scholarly journals A mathematical theory of the transcription repression (TR) therapy of cancer - whether and how it may work

Oncotarget ◽  
2017 ◽  
Vol 8 (24) ◽  
pp. 38642-38649 ◽  
Author(s):  
Yuxin Chen ◽  
Haijun Wen ◽  
Chung-I Wu
Keyword(s):  
Mathematical Theory ◽  
Transcription Repression

Transcription Repression

2013 ◽  
pp. 2251-2251
Keyword(s):  
Transcription Repression

scholarly journals Mad proteins contain a dominant transcription repression domain.

1996 ◽  
Vol 16 (10) ◽  
pp. 5772-5781 ◽  
Author(s):  
D E Ayer ◽  
C D Laherty ◽  
Q A Lawrence ◽  
A P Armstrong ◽  
R N Eisenman
Keyword(s):  
Dna Binding ◽  
Transcriptional Repression ◽  
Binding Domain ◽  
Full Length ◽  
Dna Binding Domain ◽  
Interaction Domain ◽  
Transcription Repression ◽  
Helix Loop Helix ◽  
Repression Domain

Transcription repression by the basic region-helix-loop-helix-zipper (bHLHZip) protein Mad1 requires DNA binding as a ternary complex with Max and mSin3A or mSin3B, the mammalian orthologs of the Saccharomyces cerevisiae transcriptional corepressor SIN3. The interaction between Mad1 and mSin3 is mediated by three potential amphipathic alpha-helices: one in the N terminus of Mad (mSin interaction domain, or SID) and two within the second paired amphipathic helix domain (PAH2) of mSin3A. Mutations that alter the structure of the SID inhibit in vitro interaction between Mad and mSin3 and inactivate Mad's transcriptional repression activity. Here we show that a 35-residue region containing the SID represents a dominant repression domain whose activity can be transferred to a heterologous DNA binding region. A fusion protein comprising the Mad1 SID linked to a Ga14 DNA binding domain mediates repression of minimal as well as complex promoters dependent on Ga14 DNA binding sites. In addition, the SID represses the transcriptional activity of linked VP16 and c-Myc transactivation domains. When fused to a full-length c-Myc protein, the Mad1 SID specifically represses both c-Myc's transcriptional and transforming activities. Fusions between the GAL DNA binding domain and full-length mSin3 were also capable of repression. We show that the association between Mad1 and mSin3 is not only dependent on the helical SID but is also dependent on both putative helices of the mSin3 PAH2 region, suggesting that stable interaction requires all three helices. Our results indicate that the SID is necessary and sufficient for transcriptional repression mediated by the Mad protein family and that SID repression is dominant over several distinct transcriptional activators.

A strategy for dissecting the kinetics of transcription repression mechanisms

2017 ◽  
pp. 1097-1100
Author(s):  
Cristina S.D. Palma ◽  
Sofia Startceva ◽  
Ramakanth Neeli-Venkata ◽  
Marzieh Zare ◽  
Nadia S.M. Goncalves ◽  
...  
Keyword(s):  
Transcription Repression ◽  
Kinetics Of

scholarly journals Role of HU and DNA supercoiling in transcription repression: specialized nucleoprotein repression complex at gal promoters in Escherichia coli

1999 ◽  
Vol 31 (2) ◽  
pp. 451-461 ◽  
Author(s):  
Dale E. A. Lewis ◽  
Mark Geanacopoulos ◽  
Sankar Adhya
Keyword(s):  
Escherichia Coli ◽  
Dna Supercoiling ◽  
Transcription Repression ◽  
Repression Complex
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