{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ranava D"],"funding":["Studienstiftung des Deutschen Volkes","Deutsche Forschungsgemeinschaft","European Research Council","HHS | NIH | National Institute of General Medical Sciences","NIAID NIH HHS","HHS | NIH | NIAID | Division of Microbiology and Infectious Diseases, National Institute of Allergy and Infectious Diseases","NCI NIH HHS","NIGMS NIH HHS"],"pagination":["e2207257119"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9522360"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["119(39)"],"pubmed_abstract":["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 <i>Staphylococcus aureus</i>. YwlG is an uncharacterized virulence factor in <i>S. aureus</i>. 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)"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Bidirectional sequestration between a bacterial hibernation factor and a glutamate metabolizing protein."],"pmcid":["PMC9522360"],"funding_grant_id":["725085","n/a","GRK 2062","R01AI150986","R01 AI150986","R01 GM121359","P30 CA060553","R01GM121359","SCHN 1273/10","P41 GM108569"],"pubmed_authors":["Scheidler CM","Sieber SA","Schneider S","Yap MF","Fiedler M","Pfanzelt M","Ranava D"],"additional_accession":[]},"is_claimable":false,"name":"Bidirectional sequestration between a bacterial hibernation factor and a glutamate metabolizing protein.","description":"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 <i>Staphylococcus aureus</i>. YwlG is an uncharacterized virulence factor in <i>S. aureus</i>. 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)","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Sep","modification":"2026-05-27T19:13:39.204Z","creation":"2025-02-19T03:24:07.083Z"},"accession":"S-EPMC9522360","cross_references":{"pubmed":["36122228"],"doi":["10.1073/pnas.2207257119"]}}