Cryo-EM structure of the hibernating Thermus thermophilus 100S ribosome reveals a protein-mediated d...
Cryo-EM structure of the hibernating Thermus thermophilus 100S ribosome reveals a protein-mediated dimerization mechanism
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Publisher
London: Nature Publishing Group UK
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Language
English
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Publisher
London: Nature Publishing Group UK
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Contents
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 (
Tt
HPF). In this study we demonstrate high sensitivity of
Tt
100S formation to the levels of
Tt<...
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Full title
Cryo-EM structure of the hibernating Thermus thermophilus 100S ribosome reveals a protein-mediated dimerization mechanism
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TN_cdi_doaj_primary_oai_doaj_org_article_5cc48ee25d5f4ef09112efa40bc3bd60
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_5cc48ee25d5f4ef09112efa40bc3bd60
Other Identifiers
ISSN
2041-1723
E-ISSN
2041-1723
DOI
10.1038/s41467-018-06724-x
