Differences in two Pseudomonas aeruginosa cbb3 cytochrome oxidases

被引:67
作者
Comolli, JC [1 ]
Donohue, TJ [1 ]
机构
[1] Univ Wisconsin, Dept Bacteriol, Madison, WI 53706 USA
关键词
D O I
10.1046/j.1365-2958.2003.03904.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Bacterial cytochrome cbb(3) oxidases are members of the haeme-copper oxidase superfamily that are important for energy conservation by a variety of proteobacteria under oxygen-limiting conditions. The opportunistic pathogen Pseudomonas aeruginosa is unusual in possessing two operons that each potentially encode a cbb(3) oxidase (cbb(3)-1 or cbb(3)-2). Our results demonstrate that, unlike typical enzymes of this class, the cbb(3)-1 oxidase has an important metabolic function at high oxygen tensions. In highly aerated cultures, cbb(3)-1 abundance and expression were greater than that of cbb(3)-2, and only loss of cbb(3)-1 influenced growth. Also, the activity of cbb(3)-1, not cbb(3)-2, inhibited expression of the alternative oxidase CioAB and thus influenced a signal transduction pathway much like that found in the alpha-proteobacterium Rhodobacter sphaeroides. Cbb(3)-2 appeared to play a more significant role under oxygen limitation by nature of its increased abundance and expression compared to highly aerated cultures, and the regulation of the cbb(3)-2 operon by the putative iron-sulphur protein Anr. These results indicate that each of the two P. aeruginosa cbb(3) isoforms have assumed specialized energetic and regulatory roles.
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页码:1193 / 1203
页数:11
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