[Interaction of deacylated phenylalanyl tRNA from yeasts with Escherichia coli ribosomes. The role of the modified nucleotide in codon-anticodon interaction].

The method of anticodon loop replacement has been used to make derivatives of yeast tRNA(Phe)GmAAY with the substitution at the 37 position (tRNA(Phe)GAAA), and at both the anticodon (tRNA(Phe)GCAG) and the 37 position. A quantitative study of the interaction of various types of yeast deacylated tRNA: tRNA(Phe)GmAAY, tRNA(Phe)GAAA, tRNA(Phe)GCAG, and tRNA(Phe)-Y with the P site of the 70S ribosome.poly(U) complex was carried out at different Mg2+ concentrations and temperatures.

[The hierarchy of complexes and compact structures of trivaline with nucleic acids. III. Complexes of trivaline with trinucleotides forms a rod-like structure with length of about 1000 A in solution].

We demonstrated the ability of trivaline in the course of interaction with certain trinucleotides in solution to form extended fibre-like structures with lengths of up to several thousand angstroms. Such structures were observed for complexes of trivaline with both deoxyribo- and ribonucleotides with homopurine, homopyrimidine, or random sequences, with or without terminal 5'-phosphate. A model of organization of such structures is proposed.

[The use of nucleolytic enzymes (ribonucleases, polynucleotide phosphorylases and endonuclease from Serratia marcescens) for producing initial blocks of synthetic endoribonucleases].

The simplest variant of synthetic substrate-ribozyme complex has been proposed. The schemes of potential ribozyme "subunits" synthesis have been worked out: R1--GCUUGAAACAAA; R2--AAAAACUGAUGAAAGC. The macroscale synthesis of dinucleoside monophosphate ApU, GpC, CpU catalyzed by immobilized ribonucleases of different specificity and preparation of oligoadenylates by hydrolysis of poly-A in the presence of endonuclease Serratia marcescens, as well the synthesis of conservative sequences of potential ribozyme such as ApUpG, CpUpG, GpApU, ApApApG and others have been described.

[Stepwise synthesis of oligonucleotides. XXXV. Native and immobilized polynucleotide phosphorylase from Thermus thermophilus in oligoribonucleotide synthesis].

A polynucleotide phosphorylase was isolated from the Thermus thermophilus protein fractions, obtained at different steps of purification of elongation factors, and immobilized on agarose activated with cyanogen bromide and macroporous glass modified with (3,3-diethoxypropyl)triethoxysilane. The preparations of the native and immobilized enzyme catalyzed rather efficiently the addition of adenylyl and guanylyl residues to oligonucleotide primers, in contrast to the E. coli and M.