YY2 in Mouse Preimplantation Embryos and in Embryonic Stem Cells.

encodes a mammalian-specific transcription factor (YY2) that shares high homology in the zinc finger region with both YY1 and REX1/ZFP42, encoded by the and gene, respectively. In contrast to the well-established roles of the latter two in gene regulation, X chromosome inactivation and binding to specific transposable elements (TEs), much less is known about YY2, and its presence during mouse preimplantation development has not been described. As it has been reported that mouse embryonic stem cells (mESC) cannot be propagated in the absence of , the mechanistic understanding of how contributes to mESC maintenance remains only very partially characterized.

Transcription factor Yin-Yang 2 alters neuronal outgrowth in vitro.

The Yin-Yang 2 (YY2) protein is the most recently described member of the family of YY transcription factors. Despite its high structural and functional homology with the well-characterized YY1, less is known about its role in biological processes. In previous studies, we have found differential yy2 mRNA expression levels in various cell types of the murine brain.

Yin Yang 2: the great unknown within the Yin Yang 1 regulatory network.

The fundamental biological relevance of the transcription factor Yin Yang 1 (YY1) has been studied and described intensively in hundreds of publications. To date, however, only limited data of its structural and functional homologue YY2 are available. Especially, the impact of Yin Yang 2 (YY2) in the regulatory network of YY1 is almost unexplored.

Gata4 and Sp1 regulate expression of the erythropoietin receptor in cardiomyocytes.

Experimental studies indicate significant cardioprotective effects of recombinant erythropoietin (Epo) by binding to the Epo receptor (EpoR) and by inducing various molecular mechanisms, including activation of Gata4, a transcription factor that induces anti-apoptotic genes. However, specific molecular mechanisms of EpoR regulation in cardiomyocytes are unknown. We identified a 774 bp regulatory domain in the EpoR 5' flanking region by reporter gene assays in murine HL-1 cardiomyocytes.

Developmental expression profile of the YY2 gene in mice.

Background: The transcription factor Yin Yang 2 (YY2) shares a structural and functional highly homologue DNA-binding domain with the ubiquitously expressed YY1 protein, which has been implicated in regulating fundamental biological processes. However, the biological relevance of YY2 has not been identified yet.

Results: Towards the understanding of YY2 biology, we analyzed in detail the expression pattern of yy2 in various organs during embryonic and postnatal mouse development till adulthood.

Erythropoietin-receptor gene regulation in neuronal cells.

Because erythropoietin (Epo) is intensively studied as neuroprotective agent, Epo receptor (EpoR) regulation in neurons is of particular interest. Herein, we investigated molecular mechanisms of EpoR regulation in neuronal cells including the role of GATA transcription factors. First, developmental downregulation of EpoR expression in murine brain was observed.

Transcriptional activity of the novel identified human yy2 promoter is modified by DNA methylation.

The recently identified transcription factor YY2 shares important features with the well characterized YY1 zinc finger protein. Both proteins mediate activating as well as repressing transcriptional properties and bind specifically to an identical DNA consensus motif, suggesting synergistic or competitive function of both factors in controlling target genes. In fact, the human yy2 gene has evolved from a retroposed copy of yy1, unusually inserted within an intron of another gene, the membrane-bound transcription factor protease site 2 (mbtps2).

The positive aspects of stress: strain initiates domain decondensation (SIDD).

The conventional string-based bioinformatic methods of genomic sequence analysis are often insufficient to identify DNA regulatory elements, since many of these do not have a recognizable motif. Even in case a sequence pattern is known to be associated with an element it may only partially mediate its function. This suggests that properties not correlated with the details of base sequence contribute to regulation.

Enhanceosome formation over the beta interferon promoter underlies a remote-control mechanism mediated by YY1 and YY2.

The expression of beta interferon genes from humans and mice is under the immediate control of a virus-responsive element (VRE) that terminates 110 bp upstream from the transcriptional start site. Whereas a wealth of information is available for the enhanceosome that is formed on the VRE upon the signals generated by viral infection, early observations indicating the existence of other far-upstream control elements have so far remained without a molecular fundament. Guided by a computational analysis of DNA structures, we could locate three as-yet-unknown transcription factor-binding regions at -0.

Dominant genomic structures: detection and potential signal functions in the interferon-beta domain.

Eukaryotic genomes are divided into chromatin domains, which are thought to represent independent regulatory units. Typically, these domains are flanked by bordering elements that insulate the transcription unit from outside influences. Borders also demarcate the range of action for enhancer-like elements within the domain as they are formed around dominant genomic structures such as DNAse I hypersensitive sites (HS).

Co-localization of PARP-1 and lamin B in the nuclear architecture: a halo-fluorescence- and confocal-microscopy study.

A functional interaction between poly(ADP-ribose) polymerase-1 (PARP-1) and lamin B has recently been proposed by nuclear fractionation, crosslinking, and immunoprecipitation experiments. Here we use fluorescence microscopy to verify and extend these findings. We analyze nuclear halo preparations by fluorescence in situ immuno staining (FISIS), which shares attributes with traditional nuclear fractionation techniques, and by confocal laser scanning microscopy (CLSM).