Inhibition of the DNA-binding activity of Drosophila suppressor of hairless and of its human homolog, KBF2/RBP-J kappa, by direct protein-protein interaction with Drosophila hairless.

Brou, Christel; Logeat, Frédérique; Lecourtois, Magalie; Vandekerckhove, Joël; Kourilsky, Philippe; Schweisguth, François; Israël, Alain

doi:10.1101/gad.8.20.2491

Cited by 158 publications

(151 citation statements)

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“…Then, 13 positive clones were obtained. We confirmed that one of cosmid clones (noo 8) was the correct functional clone corresponded to a PCR-3 clone by nucleotide sequencing as described by Tang et al (1993) (data not shown; Amakawa et al, 1993;Brou et al, 1994;Hamaguchi et al, t989;Matsunami et al, 1989). A cosmid clone (no.…”

supporting

confidence: 57%

“…Interestingly, the same control element is also recognized by NF-kB (Nuclear factor kappa B; Singh et al, 1988) or KBF-1 (IsraEl et al, 1989). The KBF2 protein has been purified and the corresponding cDNA has been isolated (Brou et al, 1994). A search of databases revealed perfect homology with proteins that belong to the recombination signalsequence binding protein (RBP-Jk) family.…”

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confidence: 99%

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Assignment of the human gene for KBF2/RBP-Jk to chromosome 9p12-13 and 9q13 by fluorescencein situ hybridization

et al. 1997

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SummaryThe transcription factor KBF2 has been characterized as a factor that binds to the NFkB site of mouse major histocompatibility complex (MHC) class I genes and its amino acid sequence has been shown to be identical to those of members of the recombination signalsequence binding protein (RBP-Jk) family. Previous studies by Amakawa et al. (Genomics 17, 306-315, 1993) demonstrated that the functional gene is localized at human chromosome 3q25. However, in the present study we showed by in situ hybridization With the functional KBF2/ RBPJk cosmid clone that the gene is localized at 9p12-13 and 9q13, namely, at the same loci as pseudogenes that were reported previously (Zhang et al., Jpn J Human Genet 39, 391-401, 1994). Key Words KBF2, RBP-Jk, cosmid, in situ hybridizationThe major histocompatibility complex (MHC) class I antigens specified by MHC class I genes play a key role in a number of immunological processes, particularly in the recognition of foreign antigens by cytotoxic T cells and natural killer ceils of the host (Zinkernagel and Doherty, 1979). In the mouse, the promoters of the K b and L d class I MHC genes have been used as models in studies of transcription (Israel et al., 1989). A factor designated KBF2, which can bind as a monomer to conserved sequence element (TGGGGATTCCCCA) located 165 bp upstream of the initiation site of the H-2K b class I gene. Interestingly, the same

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supporting

confidence: 57%

mentioning

confidence: 99%

Assignment of the human gene for KBF2/RBP-Jk to chromosome 9p12-13 and 9q13 by fluorescencein situ hybridization

et al. 1997

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“…RBP-Jk [59] also called CBF1 or KBF2 [60] belongs to the CSL-protein family. CSL stands for CBF1 (human), [61], Suppressor of Hairless (Drosophila), [62], Lag-1 (C. elegans), [63].…”

Section: Epigenetic Regulation Of Notch Target Genesmentioning

confidence: 99%

The Notch signaling pathway: Transcriptional regulation at Notch target genes

Borggrefe

Oswald

2009

Cell. Mol. Life Sci.

575

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. The Notch gene encodes a transmembrane receptor that gave the name to the evolutionary highly conserved Notch signaling cascade. It plays a pivotal role in the regulation of many fundamental cellular processes such as proliferation, stem cell maintenance and differentiation during embryonic and adult development. After specific ligand binding, the intracellular part of the Notch receptor is cleaved off and translocates to the nucleus, where it binds to the transcription factor RBP-J. In the absence of activated Notch, RBP-J represses Notch target genes by recruiting a corepressor complex. Here, we review Notch signaling with a focus on gene regulatory events at Notch target genes. This is of utmost importance to understand Notch signaling since certain RBP-J associated cofactors and particular epigenetic marks determine the specificity of Notch target gene expression in different cell types. We subsequently summarize the current knowledge about Notch target genes and the physiological significance of Notch signaling in development and cancer.

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“…7 Previous studies of CSL orthologs from Homo sapiens (CBF-1), Mus musculus (RS-binding protein (RBP)-Jj), Drosophila melanogaster (Su(H)), and Caenorhabditis elegans (Lag-1) revealed that CSL is a sequence specific DNA binding protein that binds the consensus sequence -C/tGTGGGAA-. [8][9][10][11] DNA sequences similar to the consensus have been identified within the promoter regions of Notch target genes in organisms ranging from flies and worms to humans and even in the genomes of the herpesviruses, Epstein-Barr virus and Kaposi's sarcomaassociated herpesvirus. [12][13][14][15] However, more complicated arrangements of CSL binding sites have also been observed, for example the enhancer of split gene complex (E(spl)-C) in flies.…”

Section: Introductionmentioning

confidence: 99%

Thermodynamic and structural insights into CSL‐DNA complexes

Friedmann

Kovall

2009

Protein Science

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The Notch pathway is an intercellular signaling mechanism that plays important roles in cell fates decisions throughout the developing and adult organism. Extracellular complexation of Notch receptors with ligands ultimately results in changes in gene expression, which is regulated by the nuclear effector of the pathway, CSL (C-promoter binding factor 1 (CBF-1), suppressor of hairless (Su(H)), lin-12 and glp-1 (Lag-1)). CSL is a DNA binding protein that is involved in both repression and activation of transcription from genes that are responsive to Notch signaling. One well-characterized Notch target gene is hairy and enhancer of split-1 (HES-1), which is regulated by a promoter element consisting of two CSL binding sites oriented in a head-to-head arrangement. Although previous studies have identified in vivo and consensus binding sites for CSL, and crystal structures of these complexes have been determined, to date, a quantitative description of the energetics that underlie CSL-DNA binding is unknown. Here, we provide a thermodynamic and structural analysis of the interaction between CSL and the two individual sites that comprise the HES-1 promoter element. Our comprehensive studies that analyze binding as a function of temperature, salt, and pH reveal moderate, but distinct, differences in the affinities of CSL for the two HES-1 binding sites. Similarly, our structural results indicate that overall CSL binds both DNA sites in a similar manner; however, minor changes are observed in both the conformation of CSL and DNA. Taken together, our results provide a quantitative and biophysical basis for understanding how CSL interacts with DNA sites in vivo.

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Inhibition of the DNA-binding activity of Drosophila suppressor of hairless and of its human homolog, KBF2/RBP-J kappa, by direct protein-protein interaction with Drosophila hairless.

Abstract: We have purified the sequence-specific DNA-binding protein KBF2 and cloned the corresponding cDNA, which is derived from the previously described

Cited by 158 publications

References 44 publications

Assignment of the human gene for KBF2/RBP-Jk to chromosome 9p12-13 and 9q13 by fluorescencein situ hybridization

Assignment of the human gene for KBF2/RBP-Jk to chromosome 9p12-13 and 9q13 by fluorescencein situ hybridization

The Notch signaling pathway: Transcriptional regulation at Notch target genes

Thermodynamic and structural insights into CSL‐DNA complexes

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