{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Sundermeyer L"],"funding":["Deutsche Forschungsgemeinschaft","Agence Nationale de la Recherche","Heinrich-Heine-Universität Düsseldorf"],"pagination":["e0267722"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9769921"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["10(6)"],"pubmed_abstract":["In Corynebacterium glutamicum the protein kinase PknG phosphorylates OdhI and thereby abolishes the inhibition of 2-oxoglutarate dehydrogenase activity by unphosphorylated OdhI. Our previous studies suggested that PknG activity is controlled by the periplasmic binding protein GlnH and the transmembrane protein GlnX, because Δ<i>glnH</i> and Δ<i>glnX</i> mutants showed a growth defect on glutamine similar to that of a Δ<i>pknG</i> mutant. We have now confirmed the involvement of GlnH and GlnX in the control of OdhI phosphorylation by analyzing the OdhI phosphorylation status and glutamate secretion in Δ<i>glnH</i> and Δ<i>glnX</i> mutants and by characterizing Δ<i>glnX</i> suppressor mutants. We provide evidence for GlnH being a lipoprotein and show by isothermal titration calorimetry that "],"journal":["Microbiology spectrum"],"pubmed_title":["Characteristics of the GlnH and GlnX Signal Transduction Proteins Controlling PknG-Mediated Phosphorylation of OdhI and 2-Oxoglutarate Dehydrogenase Activity in Corynebacterium glutamicum."],"pmcid":["PMC9769921"],"funding_grant_id":["ANR-18-CE92-0003","BO 903/4-1","iGRADbio graduate program"],"pubmed_authors":["Brocker M","Bosco G","Gujar S","Bott M","Sundermeyer L","Willbold D","Bellinzoni M","Baumgart M","Weiergraber OH"],"additional_accession":[]},"is_claimable":false,"name":"Characteristics of the GlnH and GlnX Signal Transduction Proteins Controlling PknG-Mediated Phosphorylation of OdhI and 2-Oxoglutarate Dehydrogenase Activity in Corynebacterium glutamicum.","description":"In Corynebacterium glutamicum the protein kinase PknG phosphorylates OdhI and thereby abolishes the inhibition of 2-oxoglutarate dehydrogenase activity by unphosphorylated OdhI. Our previous studies suggested that PknG activity is controlled by the periplasmic binding protein GlnH and the transmembrane protein GlnX, because Δ<i>glnH</i> and Δ<i>glnX</i> mutants showed a growth defect on glutamine similar to that of a Δ<i>pknG</i> mutant. We have now confirmed the involvement of GlnH and GlnX in the control of OdhI phosphorylation by analyzing the OdhI phosphorylation status and glutamate secretion in Δ<i>glnH</i> and Δ<i>glnX</i> mutants and by characterizing Δ<i>glnX</i> suppressor mutants. We provide evidence for GlnH being a lipoprotein and show by isothermal titration calorimetry that ","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Dec","modification":"2026-06-12T09:50:54.513Z","creation":"2025-04-05T14:54:56.648Z"},"accession":"S-EPMC9769921","cross_references":{"pubmed":["36445153"],"doi":["10.1128/spectrum.02677-22"]}}