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Akademický článek

Chp1 is a dedicated chaperone at the ribosome that safeguards eEF1A biogenesis

Autor: Melania Minoia, Jany Quintana-Cordero, Katharina Jetzinger, Ilgin Eser Kotan, Kathryn Jane Turnbull, Michela Ciccarelli, Anna E. Masser, Dorina Liebers, Eloïse Gouarin, Marius Czech, Vasili Hauryliuk, Bernd Bukau, Günter Kramer, Claes Andréasson

Publikováno v: Nature Communications, Vol 15, Iss 1, Pp 1-16 (2024)

Abstract Cotranslational protein folding depends on general chaperones that engage highly diverse nascent chains at the ribosomes. Here we discover a dedicated ribosome-associated chaperone, Chp1, that rewires the cotranslational folding machinery to

Externí odkaz: https://doaj.org/article/f23814c7fcb4463299135165d37e841c

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Akademický článek

Mechanism of phage sensing and restriction by toxin-antitoxin-chaperone systems

Publikováno v: In Cell Host & Microbe 10 July 2024 32(7):1059-1073

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Akademický článek

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Akademický článek

An ancient family of SelB elongation factor-like proteins with a broad but disjunct distribution across archaea

Autor: Hauryliuk Vasili, Atkinson Gemma C, Tenson Tanel

Publikováno v: BMC Evolutionary Biology, Vol 11, Iss 1, p 22 (2011)

Abstract Background SelB is the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome. In archaea, only a subset of methanogens utilizes selenocysteine and encodes archaeal SelB (aSelB). A SelB-like (aSelBL) homolog has pre

Externí odkaz: https://doaj.org/article/5356e08c094040aaafbc806b9ed79d30

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Akademický článek

Evolution of nonstop, no-go and nonsense-mediated mRNA decay and their termination factor-derived components

Autor: Baldauf Sandra L, Atkinson Gemma C, Hauryliuk Vasili

Publikováno v: BMC Evolutionary Biology, Vol 8, Iss 1, p 290 (2008)

Abstract Background Members of the eukaryote/archaea specific eRF1 and eRF3 protein families have central roles in translation termination. They are also central to various mRNA surveillance mechanisms, together with the eRF1 paralogue Dom34p and the

Externí odkaz: https://doaj.org/article/ce15dc96df824a70ad694360a94ee918

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Akademický článek

Guanine-nucleotide exchange on ribosome-bound elongation factor G initiates the translocation of tRNAs

Autor: Ehrenberg Måns, Hauryliuk Vasili V, Zavialov Andrey V

Publikováno v: Journal of Biology, Vol 4, Iss 2, p 9 (2005)

Abstract Background During the translation of mRNA into polypeptide, elongation factor G (EF-G) catalyzes the translocation of peptidyl-tRNA from the A site to the P site of the ribosome. According to the 'classical' model, EF-G in the GTP-bound form

Externí odkaz: https://doaj.org/article/e9546f9a7f524686b7129ef04fa1df7a

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