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dc.contributor.authorYao, Huili
dc.contributor.authorJepkorir, Grace
dc.contributor.authorLovell, Scott
dc.contributor.authorNama, Pavithra Vani
dc.contributor.authorWeeratunga, Saroja Kumari
dc.contributor.authorBattaile, Kevin P.
dc.contributor.authorRivera, Mario
dc.date.accessioned2017-04-20T16:24:41Z
dc.date.available2017-04-20T16:24:41Z
dc.date.issued2011-06-14
dc.identifier.citationYao, H., Jepkorir, G., Lovell, S., Nama, P. V., Weeratunga, S., Battaile, K. P., & Rivera, M. (2011). Two distinct ferritin-like molecules in P. aeruginosa: The product of the bfrA gene is a bacterial ferritin (FtnA) not a bacterioferritin (Bfr). Biochemistry, 50(23), 5236–5248. http://doi.org/10.1021/bi2004119en_US
dc.identifier.urihttp://hdl.handle.net/1808/23754
dc.description.abstractTwo distinct types of ferritin-like molecules often coexist in bacteria, the heme binding bacterioferritins (Bfr) and the non-heme binding bacterial ferritins (Ftn). The early isolation of a ferritin-like molecule from Pseudomonas aeruginosa suggested the possibility of a bacterioferritin assembled from two different subunits [Moore, G. R., et al. (1994) Biochem. J. 304, 493–497]. Subsequent studies demonstrated the presence of two genes encoding ferritin-like molecules in P. aeruginosa, designated bfrA and bfrB, and suggested that two distinct bacterioferritins may coexist [Ma, J.-F., et al. (1999) J. Bacteriol. 181, 3730–3742]. In this report, we present structural evidence demonstrating that the product of the bfrA gene is a ferritin-like molecule not capable of binding heme that harbors a catalytically active ferroxidase center with structural properties similar to those characteristic of bacterial and archaeal Ftns and clearly distinct from those of the ferroxidase center typical of Bfrs. Consequently, the product of the bfrA gene in P. aeruginosa is a bacterial ferritin, which we propose should be termed Pa FtnA. These results, together with the previous characterization of the product of the bfrB gene as a genuine bacterioferritin (Pa BfrB) [Weeratunga, S. J., et al. (2010) Biochemistry 49, 1160–1175], indicate the coexistence of a bacterial ferritin (Pa FtnA) and a bacterioferritin (Pa BfrB) in P. aeruginosa. In agreement with this idea, we also obtained evidence demonstrating that release of iron from Pa BfrB and Pa FtnA is likely subject to different regulation in P. aerugionsa. Whereas the efficient release of iron stored in Pa FtnA requires only the input of electrons from a ferredoxin NADP reductase (Pa Fpr), the release of iron stored in Pa BfrB requires not only electron delivery by Pa Fpr but also the presence of a “regulator”, the apo form of a bacterioferritin-associated ferredoxin (apo Pa Bfd). Finally, structural analysis of iron uptake in crystallo suggests a possible pathway for the internalization of ferroxidase iron into the interior cavity of Pa FtnA.en_US
dc.publisherACSen_US
dc.rightsCopyright © 2011 American Chemical Societyen_US
dc.titleTwo Distinct Ferritin-like Molecules in Pseudomonas aeruginosa: The Product of the bfrA Gene Is a Bacterial Ferritin (FtnA) and Not a Bacterioferritin (Bfr)en_US
dc.typeArticleen_US
kusw.kuauthorYao, Huili
kusw.kuauthorJepkorir, Grace
kusw.kuauthorNama, Pavithra V.
kusw.kuauthorWeeratunga, Saroja
kusw.kuauthorRivera, Mario
kusw.kuauthorLovell, Scott
kusw.kudepartmentChemistryen_US
kusw.kudepartmentHiguchi Biosciences Centeren_US
dc.identifier.doi10.1021/bi2004119en_US
kusw.oaversionScholarly/refereed, author accepted manuscripten_US
kusw.oapolicyThis item meets KU Open Access policy criteria.en_US
dc.rights.accessrightsopenAccess


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