Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/4749
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dc.contributor.authorO'Hare, Helen M.en_GB
dc.contributor.authorDurán, Rosarioen_GB
dc.contributor.authorCerveñansky, Carlosen_GB
dc.contributor.authorBellinzoni, Marcoen_GB
dc.contributor.authorWehenkel, Anne Marieen_GB
dc.contributor.authorPritsch, Ottoen_GB
dc.contributor.authorObal, Gonzaloen_GB
dc.contributor.authorBaumgartner, Jensen_GB
dc.contributor.authorVialaret, Jéromeen_GB
dc.contributor.authorJohnsson, Kaien_GB
dc.contributor.authorAlzari, Pedro M.en_GB
dc.date.accessioned2009-12-08T16:26:12Z-
dc.date.available2009-12-08T16:26:12Z-
dc.date.issued2008-10-20en_GB
dc.identifier.citationMolecular Microbiology, 2008, 70 (6), pp. 1408-1423.en_GB
dc.identifier.issn0950-382Xen_GB
dc.identifier.urihttp://dx.doi.org/10.1111/j.1365-2958.2008.06489.xen_GB
dc.identifier.urihttp://hdl.handle.net/2381/4749-
dc.descriptionThis paper was published as Molecular Microbiology, 2008, 70 (6), pp. 1408-1423. The definitive version is available at www3.interscience.wiley.com. Doi: 10.1111/j.1365-2958.2008.06489.xen_GB
dc.descriptionMetadata only entryen_GB
dc.description.abstractProtein kinase G of Mycobacterium tuberculosis has been implicated in virulence and in regulation of glutamate metabolism. Here we show that this kinase undergoes a pattern of autophosphorylation that is distinct from that of other M. tuberculosis protein kinases characterized to date and we identify GarA as a substrate for phosphorylation by PknG. Autophosphorylation of PknG has little effect on kinase activity but promotes binding to GarA, an interaction that is also detected in living mycobacteria. PknG phosphorylates GarA at threonine 21, adjacent to the residue phosphorylated by PknB (T22), and these two phosphorylation events are mutually exclusive. Like the homologue OdhI from Corynebacterium glutamicum, the unphosphorylated form of GarA is shown to inhibit α-ketoglutarate decarboxylase in the TCA cycle. Additionally GarA is found to bind and modulate the activity of a large NAD+-specific glutamate dehydrogenase with an unusually low affinity for glutamate. Previous reports of a defect in glutamate metabolism caused by pknG deletion may thus be explained by the effect of unphosphorylated GarA on these two enzyme activities, which may also contribute to the attenuation of virulence.en_GB
dc.formatMetadataen_GB
dc.language.isoenen_GB
dc.publisherWiley-Blackwellen_GB
dc.titleRegulation of glutamate metabolism by protein kinases in mycobacteriaen_GB
dc.typeArticleen_GB
Appears in Collections:Published Articles, Dept. of Infection, Immunity and Inflammation

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