Zobrazeno 1 - 10
of 94
pro vyhledávání: '"Andrei A Korostelev"'
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
Publikováno v:
eLife, Vol 8 (2019)
Protein synthesis ends when a ribosome reaches an mRNA stop codon. Release factors (RFs) decode the stop codon, hydrolyze peptidyl-tRNA to release the nascent protein, and then dissociate to allow ribosome recycling. To visualize termination by RF2,
Externí odkaz:
https://doaj.org/article/0da449cd4d5640eea3f29f0c324f4e4b
Autor:
Gabriel Demo, Aviram Rasouly, Nikita Vasilyev, Vladimir Svetlov, Anna B Loveland, Ruben Diaz-Avalos, Nikolaus Grigorieff, Evgeny Nudler, Andrei A Korostelev
Publikováno v:
eLife, Vol 6 (2017)
In bacteria, mRNA transcription and translation are coupled to coordinate optimal gene expression and maintain genome stability. Coupling is thought to involve direct interactions between RNA polymerase (RNAP) and the translational machinery. We pres
Externí odkaz:
https://doaj.org/article/f6133fee95ef45eba7820b5d222d7c09
Autor:
Gabriel Demo, Egor Svidritskiy, Rohini Madireddy, Ruben Diaz-Avalos, Timothy Grant, Nikolaus Grigorieff, Duncan Sousa, Andrei A Korostelev
Publikováno v:
eLife, Vol 6 (2017)
ArfA rescues ribosomes stalled on truncated mRNAs by recruiting release factor RF2, which normally binds stop codons to catalyze peptide release. We report two 3.2 Å resolution cryo-EM structures – determined from a single sample – of the 70S ri
Externí odkaz:
https://doaj.org/article/dc494d4c0f024a0eb43826dc548ad6c9
Autor:
Anna B Loveland, Eugene Bah, Rohini Madireddy, Ying Zhang, Axel F Brilot, Nikolaus Grigorieff, Andrei A Korostelev
Publikováno v:
eLife, Vol 5 (2016)
Stringent response is a conserved bacterial stress response underlying virulence and antibiotic resistance. RelA/SpoT-homolog proteins synthesize transcriptional modulators (p)ppGpp, allowing bacteria to adapt to stress. RelA is activated during amin
Externí odkaz:
https://doaj.org/article/e2ce5e5ca22a4cc7896a95764e229e8b
Publikováno v:
eLife, Vol 5 (2016)
Internal ribosome entry sites (IRESs) mediate cap-independent translation of viral mRNAs. Using electron cryo-microscopy of a single specimen, we present five ribosome structures formed with the Taura syndrome virus IRES and translocase eEF2•GTP bo
Externí odkaz:
https://doaj.org/article/092313fab65b4ba99f1e6a1f6dc57e6c
Publikováno v:
Frontiers in Microbiology, Vol 15 (2024)
Ribosomes stall on truncated or otherwise damaged mRNAs. Bacteria rely on ribosome rescue mechanisms to replenish the pool of ribosomes available for translation. Trans-translation, the main ribosome-rescue pathway, uses a circular hybrid transfer-me
Externí odkaz:
https://doaj.org/article/0843585891bd4bfc81d5f89c22600307
Autor:
Christine E. Carbone, Anna B. Loveland, Howard B. Gamper, Ya-Ming Hou, Gabriel Demo, Andrei A. Korostelev
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
EF-G drives ribosomal translocation along mRNA. Time-resolved cryo-EM captured translocation with EF-G•GTP—without inhibitors—revealing how EF-G uses ribosome fluctuations to drive translocation and GTP hydrolysis to leave at the right moment.
Externí odkaz:
https://doaj.org/article/4bea5e8abd3d4ecd81046f7ade0b17b2
Autor:
Gabriel Demo, Howard B. Gamper, Anna B. Loveland, Isao Masuda, Christine E. Carbone, Egor Svidritskiy, Ya-Ming Hou, Andrei A. Korostelev
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Translational frameshifting is a mechanism that expands the coding capabilities of mRNA. Here, structures of 70S ribosome complexes with GTPase elongation factor G (EF-G), a +1-frameshifting-prone mRNA and tRNAs reveal the cooperation between the rib
Externí odkaz:
https://doaj.org/article/9e96fbbefbf946cca2e64e5aa10017b3
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-9 (2020)
Alternative rescue factor B (ArfB) is an enzyme that releases peptides from stalled ribosomes to allow ribosome recycling. Here the authors carry-out cryo-EM analyses of 70S ribosomes complexed with ArfB on either a short or longer mRNA to reveal dis
Externí odkaz:
https://doaj.org/article/7ffabda129144820b3a56d356ee51d8b