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BIOLOGICAL CHARACTERIZATION OF TWO PUTATIVE DNA METABOLISM ENZYMES IN DEINOCOCCUS RADIODURANS

dc.contributor.advisorJulin, Douglasen_US
dc.contributor.authorMueller, Charlesen_US
dc.date.accessioned2015-02-05T06:35:19Z
dc.date.available2015-02-05T06:35:19Z
dc.date.issued2014en_US
dc.identifierhttps://doi.org/10.13016/M2589C
dc.identifier.urihttp://hdl.handle.net/1903/16082
dc.description.abstractHerA proteins are members of the FtsK-HerA superfamily of P-loop ATPases. FtsK is a bacterial protein that translocates double-stranded DNA during cell division. In archaea, herA is an essential gene that encodes an enzyme believed to be important for recombinational DNA repair. It is typically found in an operon with a gene that codes for a nuclease, nurA. Homologs of herA and nurA are found in a few bacterial genomes. In most cases, these bacteria lack an ftsK homolog. The functions of NurA and HerA in bacteria are not known. We chose to investigate the roles of NurA and HerA in Deinococcus radiodurans, typically studied for its extreme resistance to double-strand DNA breaks. The D. radiodurans genome has homologs of nurA and herA in an operon, and it also has an ftsK gene. We made strains with deletions of either herA or nurA and characterized their sensitivity to DNA damaging agents and basic growth properties. The results indicate that neither gene is essential in D. radiodurans, and deletions of the genes do not cause significant sensitivity to DNA damaging agents. The herA deletion strain displayed a distinct phenotype consisting of slower growth and larger cell types. The herA phenotype in D. radiodurans is similar to that of mutation of ftsK homologs in Escherichia coli and Bacillus subtilis. The results suggest that HerA has an FtsK-like function in cell division, rather than acting in DNA repair, in D. radiodurans.en_US
dc.language.isoenen_US
dc.titleBIOLOGICAL CHARACTERIZATION OF TWO PUTATIVE DNA METABOLISM ENZYMES IN DEINOCOCCUS RADIODURANSen_US
dc.typeDissertationen_US
dc.contributor.publisherDigital Repository at the University of Marylanden_US
dc.contributor.publisherUniversity of Maryland (College Park, Md.)en_US
dc.contributor.departmentBiochemistryen_US
dc.subject.pqcontrolledBiochemistryen_US
dc.subject.pqcontrolledMicrobiologyen_US
dc.subject.pqcontrolledMolecular biologyen_US
dc.subject.pquncontrolledDeinococcusen_US
dc.subject.pquncontrolledDNAen_US
dc.subject.pquncontrolledFtsKen_US
dc.subject.pquncontrolledHerAen_US
dc.subject.pquncontrolledNurAen_US
dc.subject.pquncontrolledRepairen_US


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