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 |
|