Interactions of Nucleosomes with Acidic Patch-Binding Peptides: A Combined Structural Bioinformatics, Molecular Modeling, Fluorescence Polarization, and Single-Molecule FRET Study.

In eukaryotic organisms, genomic DNA associates with histone proteins to form nucleosomes. Nucleosomes provide a basis for genome compaction, epigenetic markup, and mediate interactions of nuclear proteins with their target DNA loci. A negatively charged (acidic) patch located on the H2A-H2B histone dimer is a characteristic feature of the nucleosomal surface.

[The classification of ileostomies].

From experience in the treatment of 527 patients the authors suggested an original classification of ileostomy. The systematization was based on the following criteria: the object of ileostomy, the shape and method for formation of the opening, the peculiarities of its construction, localization, functions, as well as the nature of complications linked with ileostomy. The suggested classification takes into account the modern concept on artificially formed intestinal fistulas, and gives a complete idea of patients with ileostomy.

[Cloning of the locus encoding synthesis of an outer membrane protein (Omp2) of the calcium dependence plasmid of Yersinia pestis (Lehmann, Neumann)].

The genetic locus of Yersinia pestis encoding synthesis of a 46-kDa heat-inducible outer membrane protein (Omp2) was cloned into pBR322 plasmid. The Omp2 was shown to be analogous to previously described YopH and Yop2b proteins. The fifth HindIII fragment of 48-MDa calcium dependence plasmid pCad358 mediates production of 31- and 28-kDa proteins, irrespective of orientation of the insertion.

[The role of IS-elements of Yersinia pestis (Lehmann, Neumann) in the emergence of calcium-independent mutations].

Calcium independent mutants of two Yersinia pestis strains were studied. Insertions of IS100 element at three different sites of plasmid pCad within calcium dependence region were detected in Y. pestis EV, as well as two extensive deletions covering the whole region.