Abstract:
:Alternative oxidase (AOX) is a respiratory oxidase found in certain eukaryotes and bacteria; however, its role in bacterial physiology is unclear. Exploiting the genetic tractability of the bacterium Vibrio fischeri, we explore the regulation of aox expression and AOX function. Using quantitative PCR and reporter assays, we demonstrate that aox expression is induced in the presence of nitric oxide (NO), and that the NO-responsive regulatory protein NsrR mediates the response. We have identified key amino acid residues important for NsrR function and experimentally confirmed a bioinformatically predicted NsrR binding site upstream of aox. Microrespirometry demonstrated that oxygen consumption by V. fischeri CydAB quinol oxidase is inhibited by NO treatment, whereas oxygen consumption by AOX is less sensitive to NO. NADH oxidation assays using inverted membrane vesicles confirmed that NO directly inhibits CydAB, and that AOX is resistant to NO inhibition. These results indicate a role for V. fischeri AOX in aerobic respiration during NO stress.
journal_name
Mol Microbioljournal_title
Molecular microbiologyauthors
Dunn AK,Karr EA,Wang Y,Batton AR,Ruby EG,Stabb EVdoi
10.1111/j.1365-2958.2010.07194.xsubject
Has Abstractpub_date
2010-07-01 00:00:00pages
44-55issue
1eissn
0950-382Xissn
1365-2958pii
MMI7194journal_volume
77pub_type
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