scholarly journals foxD5a, a Xenopus Winged Helix Gene, Maintains an Immature Neural Ectoderm via Transcriptional Repression That Is Dependent on the C-Terminal Domain

2001 ◽  
Vol 232 (2) ◽  
pp. 439-457 ◽  
Author(s):  
Steven A. Sullivan ◽  
LaTania Akers ◽  
Sally A. Moody
Keyword(s):  
Transcriptional Repression ◽  
Winged Helix ◽  
Terminal Domain ◽  
Neural Ectoderm

scholarly journals A Novel Domain within the DEAD-Box Protein DP103 Is Essential for Transcriptional Repression and Helicase Activity

2003 ◽  
Vol 23 (1) ◽  
pp. 414-423 ◽  
Author(s):  
Xiaomei Yan ◽  
Jean-François Mouillet ◽  
Qinglin Ou ◽  
Yoel Sadovsky
Keyword(s):  
Transcriptional Repression ◽  
Mammalian Cells ◽  
Posttranslational Regulation ◽  
Helicase Activity ◽  
Cellular Functions ◽  
Terminal Domain ◽  
Dead Box ◽  
Wide Range ◽  
The Dead ◽  
Necessary And Sufficient

ABSTRACT Members of the DEAD-box family of helicases, distinguished by a core characteristic sequence of Asp-Glu-Ala-Asp, are expressed in a wide range of prokaryotes and eukaryotes and exhibit diverse cellular functions, including DNA transcription, recombination and repair, RNA processing, translation, and posttranslational regulation. Although ubiquitous, the function of most DEAD-box proteins is unknown. We and others have recently cloned DP103, which harbors conserved DEAD-box, helicase, and ATPase domains in its N terminus. DP103 (also termed Gemin3 and DDX20) interacts with SF-1, SMN, EBNA2, and EBNA3C in mammalian cells. Here we demonstrate that a discrete domain within the nonconserved C-terminal region of DP103 directly interacts with SF-1. This domain exhibits an autonomous repression function and is necessary and sufficient for repressing the transcriptional activity of SF-1. Furthermore, intact DP103 exhibits helicase activity. Importantly, the C-terminal domain is obligatory but not sufficient for this unwinding activity of DP103. Together, our results support a novel paradigm for transcriptional repression and demonstrate the bifunctional role of the C-terminal domain of DP103.

scholarly journals The Purine Repressor of Bacillus subtilis: a Novel Combination of Domains Adapted for Transcription Regulation

2003 ◽  
Vol 185 (14) ◽  
pp. 4087-4098 ◽  
Author(s):  
Sangita C. Sinha ◽  
Joseph Krahn ◽  
Byung Sik Shin ◽  
Diana R. Tomchick ◽  
Howard Zalkin ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Dna Binding ◽  
Dna Sequences ◽  
Sequence Motif ◽  
Charged Surface ◽  
Winged Helix ◽  
Gram Positive Bacteria ◽  
Terminal Domain ◽  
Winged Helix Domain ◽  
Positively Charged

ABSTRACT The purine repressor from Bacillus subtilis, PurR, represses transcription from a number of genes with functions in the synthesis, transport, and metabolism of purines. The 2.2-Å crystal structure of PurR reveals a two-domain protein organized as a dimer. The larger C-terminal domain belongs to the PRT structural family, in accord with a sequence motif for binding the inducer phosphoribosylpyrophosphate (PRPP). The PRT domain is fused to a smaller N-terminal domain that belongs to the winged-helix family of DNA binding proteins. A positively charged surface on the winged-helix domain likely binds specific DNA sequences in the recognition site. A second positively charged surface surrounds the PRPP site at the opposite end of the PurR dimer. Conserved amino acids in the sequences of PurR homologs in 21 gram-positive bacteria cluster on the proposed recognition surface of the winged-helix domain and around the PRPP binding site at the opposite end of the molecule, supporting a common function of DNA and PRPP binding for all of the proteins. The structure supports a binding mechanism in which extended regions of DNA interact with extensive protein surface. Unlike most PRT proteins, which are phosphoribosyltransferases (PRTases), PurR lacks catalytic activity. This is explained by a tyrosine side chain that blocks the site for a nucleophile cosubstrate in PRTases. Thus, B. subtilis has adapted an enzyme fold to serve as an effector-binding domain and has used it in a novel combination with the DNA-binding winged-helix domain as a repressor of purine genes.

scholarly journals Regulation of Gene Transcription by the Histone H2A N-Terminal Domain

2007 ◽  
Vol 27 (21) ◽  
pp. 7641-7648 ◽  
Author(s):  
Michael A. Parra ◽  
John J. Wyrick
Keyword(s):  
Gene Transcription ◽  
Microarray Data ◽  
Transcriptional Repression ◽  
Dna Microarrays ◽  
Reporter Genes ◽  
Histone H2a ◽  
Terminal Domain ◽  
Genome Wide ◽  
Genome Wide Expression

ABSTRACT Histone N-terminal domains play critical roles in regulating chromatin structure and gene transcription. Relatively little is known, however, about the role of the histone H2A N-terminal domain in transcription regulation. We have used DNA microarrays to characterize the changes in genome-wide expression caused by mutations in the N-terminal domain of histone H2A. Our results indicate that the N-terminal domain of histone H2A functions primarily to repress the transcription of a large subset of the Saccharomyces cerevisiae genome and that most of the H2A-repressed genes are also repressed by the histone H2B N-terminal domain. Using the histone H2A microarray data, we selected three reporter genes (BNA1, BNA2, and GCY1), which we subsequently used to map regions in the H2A N-terminal domain responsible for this transcriptional repression. These studies revealed that a small subdomain in the H2A N-terminal tail, comprised of residues 16 to 20, is required for the transcriptional repression of these reporter genes. Deletion of either the entire histone H2A N-terminal domain or just this small subdomain imparts sensitivity to UV irradiation. Finally, we show that two residues in this H2A subdomain, serine-17 and arginine-18, are specifically required for the transcriptional repression of the BNA2 reporter gene.

scholarly journals A Role for Groucho Tetramerization in Transcriptional Repression

1998 ◽  
Vol 18 (12) ◽  
pp. 7259-7268 ◽  
Author(s):  
Guoqing Chen ◽  
Pierre H. Nguyen ◽  
Albert J. Courey
Keyword(s):  
Transcriptional Repression ◽  
Fusion Proteins ◽  
Leucine Zipper ◽  
Point Mutations ◽  
Cross Linking ◽  
Transcriptional Repressors ◽  
Terminal Domain ◽  
Tetramerization Domain ◽  
Repeat Domain ◽  
Eukaryotic Organisms

ABSTRACT The Drosophila Groucho (Gro) protein is a corepressor required by a number of DNA-binding transcriptional repressors. Comparison of Gro with its homologues in other eukaryotic organisms reveals that Gro contains, in addition to a conserved C-terminal WD repeat domain, a conserved N-terminal domain, which has previously been implicated in transcriptional repression. We determined, via a variety of hydrodynamic measurements as well as protein cross-linking, that native Gro is a tetramer in solution and that tetramerization is mediated by two putative amphipathic α-helices (termed leucine zipper-like motifs) found in the N-terminal region. Point mutations in the leucine zipper-like motifs that block tetramerization also block repression by Gro, as assayed in cultured Drosophila cells with Gal4-Gro fusion proteins. Furthermore, the heterologous tetramerization domain from p53 fully substitutes for the Gro tetramerization domain in transcriptional repression. These findings suggest that oligomerization is essential for Gro-mediated repression and that the primary function of the conserved N-terminal domain is to mediate this oligomerization.

scholarly journals The winged-helix/forkhead protein myocyte nuclear factor β (MNF-β) forms a co-repressor complex with mammalian Sin3B

2000 ◽  
Vol 345 (2) ◽  
pp. 335-343 ◽  
Author(s):  
Quan YANG ◽  
Yanfeng KONG ◽  
Beverly ROTHERMEL ◽  
Daniel J. GARRY ◽  
Rhonda BASSEL-DUBY ◽  
...  
Keyword(s):  
Gene Family ◽  
Transcriptional Repression ◽  
Growth Regulation ◽  
Cellular Proliferation ◽  
Precursor Cells ◽  
Nuclear Factor ◽  
Winged Helix ◽  
Repressor Complex ◽  
Myocyte Nuclear Factor ◽  
Myogenic Precursor

Winged-helix/forkhead proteins regulate developmental events in both invertebrate and vertebrate organisms, but biochemical functions that establish a mechanism of action have been defined for only a few members of this extensive gene family. Here we demonstrate that MNF (myocyte nuclear factor)-β, a winged-helix protein expressed selectively and transiently in myogenic precursor cells of the heart and skeletal muscles, collaborates with proteins of the mammalian Sin3 (mSin3) family to repress transcription. Mutated forms of MNF-β that fail to bind mSin3 are defective in transcriptional repression and in negative growth regulation, an overexpression phenotype revealed in oncogenic transformation assays. These data extend the known repertoire of transcription factors with which mSin3 proteins can function as co-repressors to include members of the winged-helix gene family. Transcriptional repression by MNF-β-mSin3 complexes may contribute to the co-ordination of cellular proliferation and terminal differentiation of myogenic precursor cells.

scholarly journals The SAM domain-containing protein 1 (SAMD1) acts as a repressive chromatin regulator at unmethylated CpG islands

2021 ◽  
Vol 7 (20) ◽  
pp. eabf2229
Author(s):  
Bastian Stielow ◽  
Yuqiao Zhou ◽  
Yinghua Cao ◽  
Clara Simon ◽  
Hans-Martin Pogoda ◽  
...  
Keyword(s):  
Transcriptional Repression ◽  
Cpg Islands ◽  
Winged Helix ◽  
Sam Domain ◽  
Genome Wide ◽  
Chromatin Regulator ◽  
A Genome ◽  
Dna Elements ◽  
Regulatory Dna ◽  
Winged Helix Domain

CpG islands (CGIs) are key regulatory DNA elements at most promoters, but how they influence the chromatin status and transcription remains elusive. Here, we identify and characterize SAMD1 (SAM domain-containing protein 1) as an unmethylated CGI-binding protein. SAMD1 has an atypical winged-helix domain that directly recognizes unmethylated CpG-containing DNA via simultaneous interactions with both the major and the minor groove. The SAM domain interacts with L3MBTL3, but it can also homopolymerize into a closed pentameric ring. At a genome-wide level, SAMD1 localizes to H3K4me3-decorated CGIs, where it acts as a repressor. SAMD1 tethers L3MBTL3 to chromatin and interacts with the KDM1A histone demethylase complex to modulate H3K4me2 and H3K4me3 levels at CGIs, thereby providing a mechanism for SAMD1-mediated transcriptional repression. The absence of SAMD1 impairs ES cell differentiation processes, leading to misregulation of key biological pathways. Together, our work establishes SAMD1 as a newly identified chromatin regulator acting at unmethylated CGIs.

scholarly journals Structure of the Cdt1 C-terminal domain: Conservation of the winged helix fold in replication licensing factors

2009 ◽  
Vol 18 (11) ◽  
pp. 2252-2264 ◽  
Author(s):  
Bulat I. Khayrutdinov ◽  
Won Jin Bae ◽  
Young Mi Yun ◽  
Jie Hye Lee ◽  
Takashi Tsuyama ◽  
...  
Keyword(s):  
Winged Helix ◽  
Terminal Domain ◽  
Domain Conservation

scholarly journals Two domains of p53 interact with the TATA-binding protein, and the adenovirus 13S E1A protein disrupts the association, relieving p53-mediated transcriptional repression.

1995 ◽  
Vol 15 (1) ◽  
pp. 227-234 ◽  
Author(s):  
N Horikoshi ◽  
A Usheva ◽  
J Chen ◽  
A J Levine ◽  
R Weinmann ◽  
...  
Keyword(s):  
Amino Acids ◽  
Transcriptional Activation ◽  
Transcriptional Repression ◽  
Binding Protein ◽  
Direct Interaction ◽  
Tata Binding Protein ◽  
Amino Terminal ◽  
Terminal Domain ◽  
Carboxy Terminal

The tumor suppressor gene product p53 can activate and repress transcription. Both transcriptional activation and repression are thought to involve the direct interaction of p53 with the basal transcriptional machinery. Previous work has demonstrated an in vitro interaction between p53 and the TATA-binding protein that requires amino acids 20 to 57 of p53 and amino acids 220 to 271 of the TATA-binding protein. The present results show that a 75-amino-acid segment from the carboxy terminus of p53 also can bind to the TATA-binding protein in vitro, and this interaction requires amino acids 217 to 268 of the TATA-binding protein, essentially the same domain that is required for interaction with the amino-terminal domain of p53. A carboxy-terminal segment of p53 can mediate repression when bound to DNA as a GAL4-p53 fusion protein. The amino- and carboxy-terminal p53 interactions occur within the domain on the TATA-binding protein to which the adenovirus 13S E1A oncoprotein has previously been shown to bind. The 13S E1A oncoprotein can dissociate the complex formed between the carboxy-terminal domain of p53 and the TATA-binding protein and relieve p53-mediated transcriptional repression. These results demonstrate that two independent domains of p53 can potentially interact with the TATA-binding protein, and they define a mechanism--relief of repression--by which the 13S E1A oncoprotein can activate transcription through the TATA motif.

Transcriptional repression by COUP-TF II is dependent on the C-terminal domain and involves the N-CoR variant, RIP13δ1

1997 ◽  
Vol 63 (4-6) ◽  
pp. 165-174 ◽  
Author(s):  
Peter J. Bailey ◽  
Dennis H. Dowhan ◽  
Katrina Franke ◽  
Les J. Burke ◽  
Michael Downes ◽  
...  
Keyword(s):  
Transcriptional Repression ◽  
Terminal Domain
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