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dc.contributor.authorSharma A.-
dc.contributor.authorDubey V.-
dc.contributor.authorSharma R.-
dc.contributor.authorDevnath K.-
dc.contributor.authorGupta V.K.-
dc.contributor.authorAkhter J.-
dc.contributor.authorBhando T.-
dc.contributor.authorVerma A.-
dc.contributor.authorAmbatipudi, Kiran S.-
dc.contributor.authorSarkar M.-
dc.contributor.authorPathania, R.-
dc.date.accessioned2020-09-30T11:32:39Z-
dc.date.available2020-09-30T11:32:39Z-
dc.date.issued2018-
dc.identifier.citationJournal of Biological Chemistry(2018), 293(35): 13377-13388-
dc.identifier.issn219258-
dc.identifier.other30002121-
dc.identifier.urihttps://doi.org/10.1074/jbc.RA118.002921-
dc.identifier.urihttp://repository.iitr.ac.in/handle/123456789/1083-
dc.description.abstractAcinetobacter baumannii is a Gram-negative nosocomial pathogen that causes soft tissue infections in patients who spend a long time in intensive care units. This recalcitrant bacterium is very well known for developing rapid drug resistance, which is a combined outcome of its natural competence and mobile genetic elements. Successful efforts to treat these infections would be aided by additional information on the physiology of A. baumannii. Toward that end, we recently reported on a small RNA (sRNA), AbsR25, in this bacterium that regulates the genes of several efflux pumps. Because sRNAs often require the RNA chaperone Hfq for assistance in binding to their cognate mRNA targets, we identified and characterized this protein in A. baumannii. The homolog in A. baumannii is a large protein with an extended C terminus unlike Hfqs in other Gram-negative pathogens. The extension has a compositional bias toward glycine and, to a lower extent, phenylalanine and glutamine, suggestive of an intrinsically disordered region. We studied the importance of this glycine-rich tail using truncated versions of Hfq in biophysical assays and complementation of an hfq deletion mutant, finding that the tail was necessary for high-affinity RNA binding. Further tests implicate Hfq in important cellular processes of A. baumannii like metabolism, drug resistance, stress tolerance, and virulence. Our findings underline the importance of the glycine-rich C terminus in RNA binding, ribo-regulation, and auto-regulation of Hfq, demonstrating this hitherto overlooked protein motif to be an indispensable part of the A. baumannii Hfq. © 2018 Sharma et al.-
dc.language.isoen_US-
dc.publisherAmerican Society for Biochemistry and Molecular Biology Inc.-
dc.relation.ispartofJournal of Biological Chemistry-
dc.titleThe unusual glycine-rich C terminus of the Acinetobacter baumannii RNA chaperone Hfq plays an important role in bacterial physiology-
dc.typeArticle-
dc.scopusid55605770480-
dc.scopusid57203661886-
dc.scopusid57212897407-
dc.scopusid57203655760-
dc.scopusid57196262614-
dc.scopusid57201851128-
dc.scopusid56266736600-
dc.scopusid57188847653-
dc.scopusid14628506400-
dc.scopusid57196671769-
dc.scopusid7004308029-
dc.affiliationSharma, A., Department of Biotechnology, Indian Institute of Technology Roorkee, Roorkee, 247667, India-
dc.affiliationDubey, V., Department of Biotechnology, Indian Institute of Technology Roorkee, Roorkee, 247667, India-
dc.affiliationSharma, R., Department of Biotechnology, Ind-
dc.description.fundingThis work was supported by Department of Biotechnology, Government of India, Grant BT/PR11943/MED/29/874/2014; Ministry of Human Resource Development, Government of India, Ph.D. support fellowships (to A. S., R. S., T. B., and A. V.); a grant from the Dep-
dc.description.correspondingauthorPathania, R.; Department of Biotechnology, Indian Institute of Technology RoorkeeIndia; email: rpathfbs@iitr.ac.in-
Appears in Collections:Journal Publications [BT]

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