Wheat and maize miRNAs are potential regulators of human genes expression

Rakhmetullina Aizhan1, Ivashchenko Anatoliy2, Pyrkova Anna31SRI of biology and biotechnology problems Al-Farabi Kazakh National University Almaty, Kazakhstan, zhanullina1994@gmail.com2SRI of biology and biotechnology problems Al-Farabi Kazakh National University Almaty, Kazakhstan, a.iavashchenko@gmail.com3SRI of biology and biotechnology problems Al-Farabi Kazakh National University Almaty, Kazakhstan, anna.pyrkova@kaznu.kz With food, a huge variety of biological material gets into the human digestive tract, which the body uses for life support. The variety of food material entering the gastrointestinal tract, especially at the molecular level, cannot be distinguished from endogenous metabolites and these exogenous compounds can significantly alter the body\’s metabolism. Such compounds include plant miRNAs, which are indistinguishable from endogenous human miRNAs in physicochemical properties. It is necessary to clarify the degree of influence of exogenous plant miRNAs on the expression of human genes, since it is not known in advance what consequences can occur when plant miRNAs enters the human body. A huge amount of research does not allow experiments with all human genes and all plant miRNAs, so we have studied the effect of wheat and maize miRNAs on human genes using computer methods. As a result of studying the binding of 125 tae-miRNAs and 325 zma-miRNAs to mRNAs of 17508 human genes it was revealed that 158 genes were targets for 52 tae-miRNAs and 51 genes for 11 zma-miRNAs. Binding sites in the mRNA of human genes were located in 5\’UTR, CDS, 3\’UTR.

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The characteristics of interaction of miRNA with mRNA of C2H2, ERF and GRAS transcription factors of arabidopsis, rice and maize

Rakhmetullina Aizhan1, Turasheva Svetlana2, Pyrkova Anna31SRI of biology and biotechnology problems Al-Farabi Kazakh National University Almaty, Kazakhstan, zhanullina1994@gmail.com2SRI of biology and biotechnology problems Al-Farabi Kazakh National University Almaty, Kazakhstan, svetlana.turasheva@kaznu.kz3SRI of biology and biotechnology problems Al-Farabi Kazakh National University Almaty, Kazakhstan, anna.pyrkova@kaznu.kz The miRNA binding sites with mRNA of genes encoding C2H2, ERF, GRAS transcription factors (TFs) were identified for Arabidopsis thaliana, Oryza sativa and Zea mays. The free energy (ΔG) of interaction of miRNA with mRNA target genes, the maximum of free energy (ΔGm), the ratio ΔG/ΔGm, and location of the potential binding sites were calculated using MirTarget program. In mRNA of C2H2, ERF, GRAS genes of all studied plants, miRNA binding sites were located in the protein-coding part (CDS) and 5’-untranslated region (5’UTR). The ath-miR5658-5p, ath-miR5021-5p, osa-miR2102-5p, osa-miR5075-3p had binding sites in mRNA of three studied families, with the value of ΔG/ΔGm from 91% to 98%. The miR171a-3p had binding sites in mRNA GRAS transcription factors family of all studied plants, with the value of ΔG/ΔGm equal 100%. The nucleotide sequences of ath-miR171a-3p, osa-miR171a-3p, and zma-miR171a-3p were similar, and their quantitative characteristics of interaction with mRNA of LOC_Os02g44360.1, GRMZM2G037792_P01, and AT2G45160.1 genes, were also similar. The obtained results indicate the dependence of expression TF of C2H2, ERF, GRAS families on miRNA.  

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Modelling of Nef Interaction with ABCA1 Revealed Potential Binding Sites For Inhibitor Compounds

Poster (download) Anastasia A. Anashkina1, Yaroslav V. Tkachev2, Alexei A. Adzhubei31EIMB RAS, Moscow, Russia, nastya@eimb.ru2EIMB RAS, Moscow, Russia, yat@eimb.ru3EIMB RAS, Moscow, Russia, alexei.adzhubei@eimb.ru The effect of HIV-1 Nef protein on the demyelination of central nervous system cells is mediated by its effect on the cholesterol transporter protein ABCA1. To determine the possible interactions of Nef-ABCA1, an expert model of the cytoplasmic fragment ABCA1 was constructed and modelling of the reciprocal binding sites in the Nef and ABCA1 structures was carried out. This made it possible to determine the interface for the interaction of proteins and localize binding sites in them.

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