Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Vladimir I. Katunin"'
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
https://doi.org/10.1261/rna.5142404
Publikováno v:
Biochemistry. 41:12806-12812
The translocation step of elongation entails the coordinated movement of tRNA and mRNA on the ribosome. Translocation is promoted by elongation factor G (EF-G) and accompanied by GTP hydrolysis, which affects both translocation and turnover of EF-G.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::732cbffb8f7b4494ecb08465939ae53c
https://doi.org/10.1021/bi0264871
https://doi.org/10.1021/bi0264871
Publikováno v:
Cell
Summary Programmed –1 ribosomal frameshifting (−1PRF) is an mRNA recoding event utilized by cells to enhance the information content of the genome and to regulate gene expression. The mechanism of –1PRF and its timing during translation elongat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b13a40f2c10da60b24cba31e0404420
https://hdl.handle.net/11858/00-001M-0000-0024-1718-F11858/00-001M-0000-0023-DC71-011858/00-001M-0000-0024-1714-811858/00-001M-0000-0024-1715-6
https://hdl.handle.net/11858/00-001M-0000-0024-1718-F11858/00-001M-0000-0023-DC71-011858/00-001M-0000-0024-1714-811858/00-001M-0000-0024-1715-6
Autor:
Andreas Savelsbergh, Vladimir I. Katunin, Marina V. Rodnina, Berthold Wilden, Yu.P. Semenkov, Frank Peske, Wolfgang Wintermeyer
Publikováno v:
Molecular Biology. 35:559-568
The data on RNA-RNA interactions between the components of the E. coli translation machinery obtained by X-ray crystallography and chemical methods are compared. The approaches to the study of RNA secondary and tertiary structure are assessed. The fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2fe2169fc715121851038275f8040be7
https://doi.org/10.1023/a:1010523026531
https://doi.org/10.1023/a:1010523026531
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
https://doi.org/10.1073/pnas.96.17.9586
Publikováno v:
Nature. 385:37-41
Elongation factor G (EF-G) is a GTPase that is involved in the translocation of bacterial ribosomes along messenger RNA during protein biosynthesis. In contrast to current models, EF-G-dependent GTP hydrolysis is shown to precede, and greatly acceler
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::917e11fccaf74af85d9aef1f53d1bfc4
https://doi.org/10.1038/385037a0
https://doi.org/10.1038/385037a0
Autor:
Vladimir I. Katunin, Christian Egle, Mathias Sprinzl, Roland Kreutzer, Waltraud Zeidler, Wolfgang Wintermeyer, Marina V. Rodnina, Sofia Ribeiro, Annett Wagner
Publikováno v:
European Journal of Biochemistry. 229:596-604
His85 in Thermus thermophilus elongation factor Tu (EF-Tu) was replaced by glutamine, leucine and glycine residues, leading to [H85Q]EF-Tu, [H85L] EF-Tu and [H85G]EF-Tu, respectively. Asp81 was replaced by alanine leading to [D81A]EF-Tu, and replacem
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c6cce8889c8c7fd497475c7e1acb4bf4
https://doi.org/10.1111/j.1432-1033.1995.tb20503.x
https://doi.org/10.1111/j.1432-1033.1995.tb20503.x
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
https://doi.org/10.1007/978-3-7091-0215-2_26
Autor:
Vladimir I. Katunin, S. N. Hobbie, A. Kubarenko, E. C. Boettger, V. Post, C. Eichholz, Marina V. Rodnina, C. M. Bruell
Most of our understanding of ribosome function is based on experiments utilizing translational components from Escherichia coli. It is not clear to which extent the details of translation mechanisms derived from this single organism are true for all
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d83f00fe354ee5eda50ff7c45541bf1a
https://doi.org/10.5167/uzh-4533
https://doi.org/10.5167/uzh-4533
Autor:
Peter Pfister, Erik C. Böttger, Christian Bruell, Alexander S. Mankin, Liqun Xiong, Peter Bieling, Vladimir I. Katunin, Marina V. Rodnina, Malte Beringer
Publikováno v:
The Journal of biological chemistry. 280(43)
Peptide bond formation is the main catalytic function of the ribo-some. The mechanism of catalysis is presumed to be highly conserved in all organisms. We tested the conservation by comparing mechanistic features of the peptidyl transfer reaction on
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0d37ed516f259b5fb2059ea0c5934d78
https://pubmed.ncbi.nlm.nih.gov/16129670
https://pubmed.ncbi.nlm.nih.gov/16129670