Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Dmitry E. Burakovsky"'
Autor:
Dmitry E. Burakovsky, Timofei S. Zatsepin, M. Tomkuviene, Petr V. Sergiev, Olga A. Dontsova, Olga V. Sergeeva, Saulius Klimašauskas
Publikováno v:
Moscow University Chemistry Bulletin. 67:88-93
The possibility of using an S-adenosylmethionine analog, i.e., pent-2-en-4-ynyl S-adenosylhomocysteine (AduEnYn), as an rRNA methyltransferase cofactor has been investigated. The conditions for the cycloaddition reaction of the fluorescent label to t
Autor:
Dmitry V. Lesnyak, Irina A. Demina, Maxim S. Svetlov, Dmitry E. Burakovsky, Petr V. Sergiev, Marina V. Serebryakova, Alexey A. Bogdanov, Vadim M. Govorun, Vyacheslav A. Kolb, Olga A. Dontsova
Publikováno v:
Journal of Molecular Biology. 416:656-667
Catalysis of peptide bond formation in the peptidyl transferase center is a major enzymatic activity of the ribosome. Mutations limiting peptidyl transferase activity are mostly lethal. However, cellular processes triggered by peptidyl transferase de
Autor:
Maria Steblyanko, Marina V. Rodnina, A. V. Kubarenko, Petr V. Sergiev, Alexey A. Bogdanov, Dmitry E. Burakovsky, Olga A. Dontsova, Andrey L. Konevega
Publikováno v:
RNA
During protein synthesis, aminoacyl-tRNA (aa-tRNA) and release factors 1 and 2 (RF1 and RF2) have to bind at the catalytic center of the ribosome on the 50S subunit where they take part in peptide bond formation or peptidyl-tRNA hydrolysis, respectiv
Autor:
Andrei A. Leonov, Sergey V. Kiparisov, Olga A. Dontsova, Petr V. Sergiev, A. S. Smirnova, Dmitry V. Lesnyak, Dmitry E. Burakovsky, Alexey A. Bogdanov
Publikováno v:
Molecular Biology. 41:939-948
The noncanonical pairing of C2475 with G2529 links 23S rRNA helices 89 and 91 in the Escherichia coli ribosome. These nucleotides are at the intersection of the peptidyltransferase center, the sarcin-ricin loop, and the GTPase-associated center of th
Autor:
Sergey V. Kiparisov, Alexey A. Bogdanov, Dmitry E. Burakovsky, Olga A. Dontsova, Dmitry V. Lesnyak, Petr V. Sergiev, Andrei A. Leonov
Publikováno v:
Journal of Molecular Biology. 353:116-123
During the translocation of tRNAs and mRNA relative to the ribosome, the B1a, B1b and B1c bridges undergo the most extensive conformational changes among the bridges between the large and the small ribosomal subunits. The B1a bridge, also called the
Autor:
Dmitry V. Lesnyak, Alexey A. Bogdanov, Dmitry E. Burakovsky, Sergey V. Kiparisov, Petr V. Sergiev, Olga A. Dontsova, Andrei A. Leonov, Richard Brimacombe
Publikováno v:
Journal of Biological Chemistry. 280:31882-31889
Translocation catalyzed by elongation factor G occurs after the peptidyltransferase reaction on the large ribosomal subunit. Deacylated tRNA in the P-site stimulates multiple turnover GTPase activity of EF-G. We suggest that the allosteric signal fro
Autor:
I. Prokhorova, Ilya A. Osterman, Vadim M. Govorun, Olga A. Dontsova, Olga Pobeguts, Petr V. Sergiev, Dmitry G. Alexeev, Dmitry E. Burakovsky, Alexey A. Bogdanov, M. A. Galyamina, Sergey I. Kovalchuk, Marina V. Serebryakova, Ilya Altukhov
Publikováno v:
Scientific Reports
Ribosomes contain a number of modifications in rRNA, the function of which is unclear. Here we show--using proteomic analysis and dual fluorescence reporter in vivo assays--that m(2)G966 and m(5)C967 in 16S rRNA of Escherichia coli ribosomes are nece
Autor:
Marina V. Rodnina, I. Prokhorova, Olga A. Dontsova, Petr V. Sergiev, Olga V. Sergeeva, Dmitry E. Burakovsky, Alexey A. Bogdanov, Pohl Milón
Publikováno v:
Nucleic Acids Research
The functional centers of the ribosome in all organisms contain ribosomal RNA (rRNA) modifications, which are introduced by specialized enzymes and come at an energy cost for the cell. Surprisingly, none of the modifications tested so far was essenti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff1c2e3e5a6a19f63b2cb6aa526b92ca
https://hdl.handle.net/11858/00-001M-0000-000E-F17A-211858/00-001M-0000-000E-F179-411858/00-001M-0000-000F-C712-E
https://hdl.handle.net/11858/00-001M-0000-000E-F17A-211858/00-001M-0000-000E-F179-411858/00-001M-0000-000F-C712-E
Autor:
Alexey A. Bogdanov, Petr V. Sergiev, Olga A. Dontsova, Dmitry E. Burakovsky, Andrey L. Konevega, Maria Steblyanko
Publikováno v:
FEBS Letters
Helix 89 of the 23S rRNA connects ribosomal peptidyltransferase center and elongation factor binding site. Secondary structure of helix 89 determined by X-ray structural analysis involves less base pairs then could be drawn for the helix of the same
Autor:
Alexey A. Bogdanov, I. Prokhorova, Olga A. Dontsova, Ilya A. Osterman, Dmitry E. Burakovsky, Anna Y. Golovina, Olga V. Sergeeva, Petr V. Sergiev, Mikhail V. Nesterchuk
Publikováno v:
Ribosomes ISBN: 9783709102145
Modified nucleosides are present in all kinds of stable RNA molecules, tRNAs being particularly rich in them (Auffinger and Westhof, 1998). Ribosomal RNA (rRNA) from all organisms contains modifications, and there is a correlation between the overall
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fa814ef1a9c08bfdf493fb5abe283f9e
https://doi.org/10.1007/978-3-7091-0215-2_9
https://doi.org/10.1007/978-3-7091-0215-2_9