Výsledky vyhledávání - "Yuri P. Semenkov"

Spontaneous reverse movement of mRNA-bound tRNA through the ribosome

Autor: Holger Stark, Marina V. Rodnina, Yuri P. Semenkov, Niels Fischer, Andrey L. Konevega, Wolfgang Wintermeyer

Publikováno v: Nature Structural & Molecular Biology. 14:318-324

During the translocation step of protein synthesis, a complex of two transfer RNAs bound to messenger RNA (tRNA-mRNA) moves through the ribosome. The reaction is promoted by an elongation factor, called EF-G in bacteria, which, powered by GTP hydroly

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::496df31ea8f9fc6841ce12e88e395d0d
https://doi.org/10.1038/nsmb1221

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Purine bases at position 37 of tRNA stabilize codon–anticodon interaction in the ribosomal A site by stacking and Mg2+-dependent interactions

Autor: Natalia G. Soboleva, Vladimir I. Katunin, Marina V. Rodnina, Makhno Vi, Andrey L. Konevega, Wolfgang Wintermeyer, Yuri P. Semenkov

Publikováno v: RNA

The anticodon loop of tRNA contains a number of conserved or semiconserved nucleotides. In most tRNAs, a highly modified purine is found at position 37 immediately 3′ to the anticodon. Here, we examined the role of the base at position 37 for tRNAP

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b2bf1b82732ef1f61967afbcd1af1c7e
https://doi.org/10.1261/rna.5142404

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[Untitled]

Autor: Wolfgang Wintermeyer, Marina V. Rodnina, Yuri P. Semenkov

Publikováno v: Nature Structural Biology. 7:1027-1031

Upon transpeptidylation, the 3′ end of aminoacyl-tRNA (aa-tRNA) in the ribosomal A site enters the A/P hybrid state. We report that transpeptidylation of Phe-tRNA to fMetPhe-tRNA on Escherichia coli ribosomes substantially lowers the kinetic stabil

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::395b9e5bcea933035e623b906ebdf5cc
https://doi.org/10.1038/80938

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Thiostrepton inhibits the turnover but not the GTPase of elongation factor G on the ribosome

Autor: Vladimir I. Katunin, Andreas Savelsbergh, Wolfgang Wintermeyer, Yuri P. Semenkov, Marina V. Rodnina, Natalia B. Matassova

Publikováno v: Proceedings of the National Academy of Science of the United States of America

The region around position 1067 in domain II of 23S rRNA frequently is referred to as the GTPase center of the ribosome. The notion is based on the observation that the binding of the antibiotic thiostrepton to this region inhibited GTP hydrolysis by

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3c01189ed1f1aad2c18a66a11153513
https://doi.org/10.1073/pnas.96.17.9586

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Functions of elongation factor G in translocation and ribosome recycling

Autor: Andreas Savelsbergh, Frank Peske, Wolfgang Wintermeyer, Niels Fischer, Holger Stark, Marina V. Rodnina, Vladimir I. Katunin, Andrey L. Konevega, Yuri P. Semenkov

Publikováno v: Ribosomes ISBN: 9783709102145

Among the translation factors that assist the ribosome in synthesizing proteins, elongation factor G (EF-G) is the only one that functions in two different phases of protein synthesis, i. e. in the translocation step of the elongation phase and in ri

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::35fb6b4ee8b159140dcf114008f4c3fd
https://doi.org/10.1007/978-3-7091-0215-2_26

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Conformation of 4.5S RNA in the signal recognition particle and on the 30S ribosomal subunit

Autor: Jens Warnecke, Marina V. Rodnina, Johannes Jöckel, Yuri P. Semenkov, Philipp Beinker, Shan-Qing Gu, Wolfgang Wintermeyer

Publikováno v: RNA

The signal recognition particle (SRP) from Escherichia coli consists of 4.5S RNA and protein Ffh. It is essential for targeting ribosomes that are translating integral membrane proteins to the translocation pore in the plasma membrane. Independently

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::95e8790d6e62b7c6a6eb3f7e3f3d9119
https://hdl.handle.net/11858/00-001M-0000-002D-2322-111858/00-001M-0000-002D-2324-E

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The 'allosteric three-site model' of elongation cannot be confirmed in a well-defined ribosome system from Escherichia coli

Autor: Yuri P. Semenkov, Marina V. Rodnina, Wolfgang Wintermeyer

For the functional role of the ribosomal tRNA exit (E) site, two different models have been proposed. It has been suggested that transient E-site binding of the tRNA leaving the peptidyl (P) site promotes elongation factor G (EF-G)-dependent transloc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cdd436e24e20d74712ea7edebd8fefcc
https://europepmc.org/articles/PMC37964/

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Interaction of tRNA with the A and P sites of rabbit-liver 80S ribosomes and their 40S subunits

Autor: Anna V. El'skaya, Marina V. Rodnina, S.V. Kirillov, Yuri P. Semenkov

Publikováno v: European Journal of Biochemistry

The interaction between tRNA and rabbit liver 80S ribosomes and 40S subunits was studied using a nitrocellulose membrane filtration technique. Binding of the different tRNA forms (aminoacyl-, peptidyl- or deacylated) to poly(U)-programmed 40S subunit

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a8eaf6b89d3d8bf903018a2f59c38c23
https://hdl.handle.net/11858/00-001M-0000-002B-AFDC-411858/00-001M-0000-002B-AFDA-8

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