Analysis of DNA-protein interactions in complexes of transcription factor NF-kappaB with DNA.

We have applied bioinformatic analysis of X-ray 3D structures of complexes of transcription factor NF-kappaB with DNAs. We determined the number of possible Van der Waals contacts and hydrogen bonds between amino acid residues and nucleotides. Conservative contacts in the NF-kappaB dimer-DNA complex composed of p50 and/or p65 NF-kappaB subunit and DNA sequences like 5 -GGGAMWTTCC-3 were revealed. Based on these results, we propose a novel scheme for interactions between NF-kappaB p50 homodimer and the kappaB region of the immunoglobulin light chain gene enhancer (Ig-kappaB). We applied a chemical cross-linking technique to study the proximity of some Lys and Cys residues of NF-kappaB p50 subunit with certain reactive nucleotides into its recognition site. In all cases, the experimentally determined protein-DNA contacts were in good agreement with the predicted ones.

[Current problems of delivering medical care on ships]. / Aktual'nye problemy okazaniia meditsinskoi pomoshchi na sudakh dal'nego plavaniia.

Medical personnel of ships has been liquidated during the period of public health reforms, and in accordance with International Regulations of Floating Safety, sailors now have to be trained to render first medical care and care of victims on board the ship. This paper discusses the problems essential for such training of sailors and presents the experience gained by the first worldwide department of marine medical training of sailors at S. O. Makarov State Navy Academy. Basic characteristics of navy legislation are presented. Special attention is paid to general laws and laws essential for this sphere.

Tetracyclines induce changes in accessibility of ribosomal proteins to proteases.

Limited proteolysis was used to test the interaction of tetracyclines and some of their derivatives with ribosomes. Proteolysis of the free ribosomes was compared with that of the ligand-bound ribosomes. The interaction of different tetracyclines with ribosomes depends on their chemical structure and produces both a protective effect and an increased susceptibility to proteases of some ribosomal proteins in the 30S and 50S subparticles. Most of the proteins affected by tetracycline action are located on the head of the 30S and interface side of the 50S subunits. On the grounds of the obtained data one of the antibiotic-binding regions can be located near the ribosomal peptidyl transferase center. The effect of possible conformational changes induced by tetracyclines on the translation process is discussed.