Zobrazeno 1 - 10
of 62
pro vyhledávání: '"Dmitri N Ermolenko"'
Autor:
Thareendra De Zoysa, Alayna C Hauke, Nivedita R Iyer, Erin Marcus, Sarah M Ostrowski, Franziska Stegemann, Dmitri N Ermolenko, Justin C Fay, Eric M Phizicky
Publikováno v:
PLoS Genetics, Vol 20, Iss 1, p e1011146 (2024)
tRNA modifications are crucial in all organisms to ensure tRNA folding and stability, and accurate translation. In both the yeast Saccharomyces cerevisiae and the evolutionarily distant yeast Schizosaccharomyces pombe, mutants lacking certain tRNA bo
Externí odkaz:
https://doaj.org/article/53282ce9b569489fa844b57daca8e9c0
Autor:
Chen Bao, Sarah Loerch, Clarence Ling, Andrei A Korostelev, Nikolaus Grigorieff, Dmitri N Ermolenko
Publikováno v:
eLife, Vol 9 (2020)
Although the elongating ribosome is an efficient helicase, certain mRNA stem-loop structures are known to impede ribosome movement along mRNA and stimulate programmed ribosome frameshifting via mechanisms that are not well understood. Using biochemic
Externí odkaz:
https://doaj.org/article/716549eb2dca4eb8a1914d4e9a7819df
Autor:
Chen Bao, Mingyi Zhu, Inna Nykonchuk, Hironao Wakabayashi, David H. Mathews, Dmitri N. Ermolenko
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-14 (2022)
This study shows that rather than high thermodynamic stability, specific length and structure enable regulatory mRNA stem-loops to pause translation. These findings aid identification of new regulatory mRNA stem-loops.
Externí odkaz:
https://doaj.org/article/65b9c62dcab346d481ecdf3e4f03a42e
Publikováno v:
International Journal of Molecular Sciences, Vol 24, Iss 8, p 6878 (2023)
Translational G proteins, whose release from the ribosome is triggered by GTP hydrolysis, regulate protein synthesis. Concomitantly with binding and dissociation of protein factors, translation is accompanied by forward and reverse rotation between r
Externí odkaz:
https://doaj.org/article/acf04105d9724454b2782ad4e4d1db16
Autor:
Wan-Jung C. Lai, Mohammad Kayedkhordeh, Erica V. Cornell, Elie Farah, Stanislav Bellaousov, Robert Rietmeijer, Enea Salsi, David H. Mathews, Dmitri N. Ermolenko
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-11 (2018)
It was previously suggested that formation of RNA secondary structure tends to bring the 5′ and 3′ ends of RNA into close proximity. Here the authors use experimental and computational approaches to show that mRNAs and lncRNAs have an intrinsic p
Externí odkaz:
https://doaj.org/article/4cabaeef47a048fa92dd9b55643a6ce8
Mediated by elongation factor G (EF-G), ribosome translocation along mRNA is accompanied by rotational movement between ribosomal subunits. Here, we reassess whether the intersubunit rotation requires GTP hydrolysis by EF-G or can occur spontaneously
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::aa5562aa06dff7e17d07ebbfc1ca3d78
https://doi.org/10.1101/2023.05.09.540051
https://doi.org/10.1101/2023.05.09.540051
Autor:
Anant A. Agrawal, Enea Salsi, Rakesh Chatrikhi, Steven Henderson, Jermaine L. Jenkins, Michael R. Green, Dmitri N. Ermolenko, Clara L. Kielkopf
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-14 (2016)
The pre-mRNA splicing factor U2AF65 recognizes 3′ splice sites in human gene transcripts, but the details are not fully understood. Here, the authors report U2AF65 structures and single molecule FRET that reveal mechanistic insights into splice sit
Externí odkaz:
https://doaj.org/article/c1b792d28aba471e81c175eb71e73c9e
Autor:
Dmitri N. Ermolenko, Chen Bao
Publikováno v:
Biochemistry. Biokhimiia
During protein synthesis, ribosome moves along mRNA to decode one codon after the other. Ribosome translocation is induced by a universally conserved protein, elongation factor G (EF-G) in bacteria and elongation factor 2 (EF-2) in eukaryotes. EF-G-i
Autor:
Wan-Jung C. Lai, Mingyi Zhu, Margarita Belinite, Gregory Ballard, David H. Mathews, Dmitri N. Ermolenko
Publikováno v:
Journal of molecular biology. 434(24)
The 5' cap and 3' poly(A) tail of mRNA are known to synergistically stimulate translation initiation via the formation of the cap•eIF4E•eIF4G•PABP•poly(A) complex. Most mRNA sequences have an intrinsic propensity to fold into extensive intram
Autor:
Inna Nykonchuk, Mingyi Zhu, Chen Bao, Hironao Wakabayashi, Dmitri N. Ermolenko, David H. Mathews
Publikováno v:
Nature Communications. 13
Translating ribosomes unwind mRNA secondary structures by three basepairs each elongation cycle. Despite the ribosome helicase, certain mRNA stem-loops stimulate programmed ribosomal frameshift by inhibiting translation elongation. Here, using mutage