Rv3080c regulates the rate of inhibition of mycobacteria by Isoniazid through FabD

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dc.contributor.author Kumari, Ruma
dc.contributor.author Saxena, Richa
dc.contributor.author Tiwari, Sameer
dc.contributor.author Tripathi, D K
dc.contributor.author Srivastava, K K
dc.date.accessioned 2013-03-08T09:50:57Z
dc.date.available 2013-03-08T09:50:57Z
dc.date.issued 2013
dc.identifier.citation Molecular and Cellular Biochemistry 2013, 374, (1-2) 149-155 en
dc.identifier.uri http://hdl.handle.net/123456789/1029
dc.description.abstract The mycobacterial FAS-II multienzyme complex has been identified to be a target of Ser/Thr protein kinases (STPKs) of Mycobacterium tuberculosis (MTB), with substrates, including the malonyl-CoA:ACP transacylase (FabD) and the β-ketoacyl-ACP synthases KasA and KasB. These proteins are phosphorylated by various kinases in vitro. The present study links the correlation of FASII pathway with serine threonine protein kinase of MTB. In the preliminary finding we have shown that mycobacterial protein Rv3080c (PknK) phosphorylates FabD and the knockdown of PknK protein in mycobacteria down regulates FabD expression. This event leads to the differential inhibition of mycobacteria in presence of Isoniazid (INH), as the inhibition of growth of mycobacteria in presence of INH is enhanced in PknK deficient mycobacteria. en
dc.format.extent 693573 bytes
dc.format.mimetype application/pdf
dc.language.iso en en
dc.relation.ispartofseries CDRI Communication No. 8347 en
dc.subject Mycobacteria en
dc.subject PknK en
dc.subject FabD en
dc.subject FasII en
dc.title Rv3080c regulates the rate of inhibition of mycobacteria by Isoniazid through FabD en
dc.type Article en


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