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dc.contributor.author | Flygaard R. | |
dc.contributor.author | Boegholm N. | |
dc.contributor.author | Yusupov M. | |
dc.contributor.author | Jenner L. | |
dc.date.accessioned | 2019-01-22T20:54:59Z | |
dc.date.available | 2019-01-22T20:54:59Z | |
dc.date.issued | 2018 | |
dc.identifier.uri | https://dspace.kpfu.ru/xmlui/handle/net/149402 | |
dc.description.abstract | © 2018, The Author(s). In response to cellular stresses bacteria conserve energy by dimerization of ribosomes into inactive hibernating 100S ribosome particles. Ribosome dimerization in Thermus thermophilus is facilitated by hibernation-promoting factor (TtHPF). In this study we demonstrate high sensitivity of Tt100S formation to the levels of TtHPF and show that a 1:1 ratio leads to optimal dimerization. We report structures of the T. thermophilus 100S ribosome determined by cryo-electron microscopy to average resolutions of 4.13 Å and 4.57 Å. In addition, we present a 3.28 Å high-resolution cryo-EM reconstruction of a 70S ribosome from a hibernating ribosome dimer and reveal a role for the linker region connecting the TtHPF N- and C-terminal domains in translation inhibition by preventing Shine−Dalgarno duplex formation. Our work demonstrates that species-specific differences in the dimerization interface govern the overall conformation of the 100S ribosome particle and that for Thermus thermophilus no ribosome-ribosome interactions are involved in the interface. | |
dc.title | Cryo-EM structure of the hibernating Thermus thermophilus 100S ribosome reveals a protein-mediated dimerization mechanism | |
dc.type | Article | |
dc.relation.ispartofseries-issue | 1 | |
dc.relation.ispartofseries-volume | 9 | |
dc.collection | Публикации сотрудников КФУ | |
dc.source.id | SCOPUS-2018-9-1-SID85054589371 |