S Ch Agalarov

Publications (6)9.14 Total impact

• Article: Leader sequences of eukaryotic mRNA can be simultaneously bound to initiating 80S ribosome and 40S ribosomal subunit.

  E A Sogorin, N E Shirokikh, A M Ibragimova, V D Vasiliev, S Ch Agalarov, A S Spirin
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  ABSTRACT: Binding of mRNA leader sequences to ribosomes was studied in conditions of a cell-free translation system based on wheat germ extract. Leader sequence of TMV mRNA (the so-called omega-RNA sequence) was able to bind simultaneously 80S ribosome and 40S ribosomal subunit. It was found that nucleotide substitutions in omega-RNA resulting in destabilization of RNA structure have no effect on the complex formation with both 80S ribosome and 40S ribosomal subunit. Leader sequence of globin mRNA is also able to form a similar joint complex. It is supposed that the ability of mRNA leader sequences to bind simultaneously 80S ribosome and 40S subunit is independent of leader nature and may reflect previously unknown eukaryotic mechanisms of translation initiation.
  Biochemistry (Moscow) 04/2012; 77(4):342-5. · 1.06 Impact Factor
• Article: Chemical and enzymatic probing of spatial structure of the omega leader of tobacco mosaic virus RNA.

  N E Shirokikh, S Ch Agalarov, A S Spirin
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  ABSTRACT: The 5'-untranslated sequence of tobacco mosaic virus RNA - the so-called omega leader - exhibits features of a translational enhancer of homologous and heterologous mRNAs. The absence of guanylic residues, the presence of multiple trinucleotide CAA repeats in its central region, and the low predictable probability of the formation of an extensive secondary structure of the Watson-Crick type were reported as the peculiarities of the primary structure of the omega leader. In this work we performed chemical and enzymatic probing of the secondary structure of the omega leader. The isolated RNA comprising omega leader sequence was subjected to partial modifications with dimethyl sulfate and diethyl pyrocarbonate and partial hydrolyses with RNase A and RNase V1. The sites and the intensities of the modifications or the cleavages were detected and measured by the primer extension inhibition technique. The data obtained have demonstrated that RNase A, which attacks internucleotide bonds at the 3' side of pyrimidine nucleotides, and diethyl pyrocarbonate, which modifies N7 of adenines not involved in stacking interactions, weakly affected the core region of omega leader sequence enriched with CAA-repeats, this directly indicating the existence of a stable spatial structure. The significant stability of the core region structure to RNase A and diethyl pyrocarbonate was accompanied by its complete resistance against RNase V1, which cleaves a polyribonucleotide chain involved in Watson-Crick double helices and generally all A-form RNA helices, thus being an evidence in favor of a non-Watson-Crick structure. The latter was confirmed by the full susceptibility of all adenines and cytosines of the omega polynucleotide chain to dimethyl sulfate, which exclusively modifies N1 of adenines and N3 of cytosines not involved in Watson-Crick interactions. Thus, our data have confirmed that (1) the regular (CAA)(n) sequence characteristic of the core region of the omega leader does form stable secondary structure, and (2) the structure formed is not the canonical double helix of the Watson-Crick type.
  Biochemistry (Moscow) 04/2010; 75(4):405-11. · 1.06 Impact Factor
• Article: Preparation of a 'beheaded' derivative of the 30S ribosomal subunit.

  A B Ulitin, S Ch Agalarov, I N Serdyuk
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  ABSTRACT: Oligodesoxyribonucleotide-directed cleavage of protein-deficient Thermus thermophilus derivatives of the 30S ribosomal subunits with RNase H is described. A homogeneous RNP fragment has been isolated as a result of the cleavage and subsequent purification in the sucrose gradient. It corresponds to the central and 5' domains of the 30S ribosomal subunit. The high compactness of the fragment in solution suggests that it can be considered as a 'beheaded' derivative of the 30S ribosomal subunit. The absence of a reconstitution stage in isolation of the 22S RNP fragment provides for its preparation in large amounts.
  Biochimie 10/1997; 79(8):523-6. · 3.02 Impact Factor
• Article: [Preparative isolation of proteins from 30S ribosomal subparticles from Thermus thermophilus under nondenaturing conditions].

  I A Eliseĭkina, S Ch Agalarov, T A Muranova, L F Markova, I A Kashparov, N K Avliiakulov, M B Garber
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  ABSTRACT: A procedure for isolation in preparative amounts of 15 individual proteins from ribosomal 30S subparticles of Thermus thermophilus under non-denaturing conditions, has been developed. The amino acid composition and molecular masses of the proteins have been determined and the UV absorption spectra and extinction coefficients measured. A homology of 13 proteins to corresponding ribosomal proteins of E. coli has been established.
  Biokhimii͡a (Moscow, Russia) 11/1995; 60(10):1720-30.
• Article: Crystals of protein S6 from the 30 S ribosomal subunit of Thermus thermophilus.

  S E Sedelnikova, S Ch Agalarov, I A Eliseikina, N P Fomenkova, S V Nikonov, M B Garber, L A Svensson, A Liljas
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  ABSTRACT: Crystals of protein S6 from the small ribosomal subunit of an extreme thermophile, Thermus thermophilus, have been obtained by the hanging-drop/vapor diffusion technique using methane pentanediol as a precipitant in the presence of potassium fluoride. The crystals belong to the space group C222 with cell parameters a = 106.7, b = 52.8, c = 41.0 A. They diffract to 2.0 A resolution.
  Journal of Molecular Biology 09/1991; 220(3):549-50. · 4.00 Impact Factor
• Article: On the shape and compactness of ribosomal RNAs and their complexes with proteins in solution

  I.N. Serdyuk, S. Ch. Agalarov, G.M. Gongadze, A.T. Gudkov, S.E. Sedelnikova, R.P. May, A.S. Spirin
  Molekularnaya Biologiya. 01/1984; 18:244-260.