N-methyladenosine (mA) is one of the most common modifications in both eukaryotic and prokaryotic mRNAs. It has been experimentally confirmed that mA methylation is involved in the regulation of stability and translation of various mRNAs. Until recently, the majority of mA-related studies have been focused on the cytoplasmic functions of this modification.
View Article and Find Full Text PDFDuring gastrulation and neurulation, the chordamesoderm and overlying neuroectoderm of vertebrate embryos converge under the control of a specific genetic programme to the dorsal midline, simultaneously extending along it. However, whether mechanical tensions resulting from these morphogenetic movements play a role in long-range feedback signaling that in turn regulates gene expression in the chordamesoderm and neuroectoderm is unclear. In the present work, by using a model of artificially stretched explants of midgastrula embryos and full-transcriptome sequencing, we identified genes with altered expression in response to external mechanical stretching.
View Article and Find Full Text PDFZyxin is a cytoskeletal LIM-domain protein that regulates actin cytoskeleton assembly and gene expression. In the present work, we find that zyxin downregulation in Xenopus laevis embryos reduces the expression of numerous genes that regulate cell differentiation, but it enhances that of several genes responsible for embryonic stem cell status, specifically klf4, pou5f3.1, pou5f3.
View Article and Find Full Text PDFIn this study, the optimized method for designing IgG-binding magnetosomes based on integration of IgG-binding fusion proteins into magnetosome membrane in vitro is presented. Fusion proteins Mbb and Mistbb consisting of magnetosome membrane protein MamC and membrane associating protein Mistic from Bacillus subtilis as anchors and BB-domains of Staphylococcus aureus protein A as IgG-binding region were used. With Response Surface Methodology (RSM) the highest level of proteins integration into magnetosome membrane was achieved under the following parameters: pH 8.
View Article and Find Full Text PDFThe Kaiso protein was originally described as a BTB/POZ zinc-finger transcription factor and a p120-catenin-binding partner. It is a DNA methylation-dependent transcriptional repressor, but its biological role in mice is still unknown. Here, we characterized a Kaiso-specific antibody by examining Kaiso protein distribution by immunofluorescence microscopy in the following tissues and cell types of adult mice: skin, small intestine, mammary glands, urinary bladder, and others.
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