Bidirectional sequestration between a bacterial hibernation factor and a glutamate metabolizing protein

David Ranava, Christopher M. Scheidler, Martin Pfanzelt, Michaela Fiedler, Stephan A. Sieber, Sabine Schneider, Mee Ngan F. Yap

Research output: Contribution to journalArticlepeer-review

1 Scopus citations


Bacterial hibernating 100S ribosomes (the 70S dimers) are excluded from translation and are protected from ribonucleolytic degradation, thereby promoting long-term viability and increased regrowth. No extraribosomal target of any hibernation factor has been reported. Here, we discovered a previously unrecognized binding partner (YwlG) of hibernation-promoting factor (HPF) in the human pathogen Staphylococcus aureus. YwlG is an uncharacterized virulence factor in S. aureus. We show that the HPF-YwlG interaction is direct, independent of ribosome binding, and functionally linked to cold adaptation and glucose metabolism. Consistent with the distant resemblance of YwlG to the hexameric structures of nicotinamide adenine dinucleotide (NAD)-specific glutamate dehydrogenases (GDHs), YwlG overexpression can compensate for a loss of cellular GDH activity. The reduced abundance of 100S complexes and the suppression of YwlG-dependent GDH activity provide evidence for a two-way sequestration between YwlG and HPF. These findings reveal an unexpected layer of regulation linking the biogenesis of 100S ribosomes to glutamate metabolism.

Original languageEnglish
Article numbere2207257119
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number39
StatePublished - 27 Sep 2022


  • Staphylococcus aureus
  • glutamate dehydrogenase
  • hibernation
  • moonlighting protein
  • ribosome


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