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• W1882169712 abstract "ABSTRACT We have cloned a 3.6-kb genomic DNA fragment from Pseudomonas aeruginosa harboring the rpoA , rplQ , katA , and bfrA genes. These loci are predicted to encode, respectively, (i) the α subunit of RNA polymerase; (ii) the L17 ribosomal protein; (iii) the major catalase, KatA; and (iv) one of two iron storage proteins called bacterioferritin A (BfrA; cytochrome b 1 or b 557 ). Our goal was to determine the contributions of KatA and BfrA to the resistance of P. aeruginosa to hydrogen peroxide (H 2 O 2 ). When provided on a multicopy plasmid, the P. aeruginosa katA gene complemented a catalase-deficient strain of Escherichia coli . The katA gene was found to contain two translational start codons encoding a heteromultimer of ∼160 to 170 kDa and having an apparent K m for H 2 O 2 of 44.7 mM. Isogenic katA and bfrA mutants were hypersusceptible to H 2 O 2 , while a katA bfrA double mutant demonstrated the greatest sensitivity. The katA and katA bfrA mutants possessed no detectable catalase activity. Interestingly, a bfrA mutant expressed only ∼47% the KatA activity of wild-type organisms, despite possessing wild-type katA transcription and translation. Plasmids harboring bfrA genes encoding BfrA altered at critical amino acids essential for ferroxidase activity could not restore wild-type catalase activity in the bfrA mutant. RNase protection assays revealed that katA and bfrA are on different transcripts, the levels of which are increased by both iron and H 2 O 2 . Mass spectrometry analysis of whole cells revealed no significant difference in total cellular iron levels in the bfrA , katA , and katA bfrA mutants relative to wild-type bacteria. Our results suggest that P. aeruginosa BfrA may be required as one source of iron for the heme prosthetic group of KatA and thus for protection against H 2 O 2 ." @default.
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• W1882169712 date "1999-06-15" @default.
• W1882169712 modified "2023-10-12" @default.
• W1882169712 title "Bacterioferritin A Modulates Catalase A (KatA) Activity and Resistance to Hydrogen Peroxide in <i>Pseudomonas aeruginosa</i>" @default.
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• W1882169712 doi "https://doi.org/10.1128/jb.181.12.3730-3742.1999" @default.
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