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dc.contributor.authorGhosh, Soumitra-
dc.date.accessioned2024-08-03T06:19:36Z-
dc.date.available2024-08-03T06:19:36Z-
dc.date.issued2008-09-
dc.identifier.urihttps://www.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.2008/020933-0-
dc.identifier.urihttp://dspace.bits-pilani.ac.in:8080/jspui/xmlui/handle/123456789/15081-
dc.description.abstractGlutamate racemase (MurI) provides d-glutamate, a key building block in the peptidoglycan of the bacterial cell wall. Besides having a crucial role in cell wall biosynthesis, MurI proteins from some bacteria have been shown to act as an inhibitor of DNA gyrase. Mycobacterium tuberculosis and Mycobacterium smegmatis MurI exhibit these dual characteristics. Here, we show that the two activities of M. tuberculosis MurI are unlinked and independent of each other. The racemization function of MurI is not essential for its gyrase-inhibitory property. MurI–DNA gyrase interaction influences gyrase activity but has no effect on the racemization activity of MurI. Overexpression of MurI in vivo provides resistance to the action of ciprofloxacin, suggesting the importance of the interaction in gyrase modulation. We propose that the moonlighting activity of MurI has evolved more recently than its racemase function, to play a transient yet important role in gyrase modulation.en_US
dc.language.isoenen_US
dc.publisherAmerican Society for Microbiologyen_US
dc.subjectBiologyen_US
dc.subjectAMFen_US
dc.subjectAutocrine motility factoren_US
dc.subjectCircular dichroismen_US
dc.subjectPGIen_US
dc.subjectPhosphoglucose isomeraseen_US
dc.titleMoonlighting function of glutamate racemase from Mycobacterium tuberculosis: racemization and DNA gyrase inhibition are two independent activities of the enzymeen_US
dc.typeArticleen_US
Appears in Collections:Department of Biological Sciences

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