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    Anaerobic survival of Pseudomonas aeruginosa by pyruvate fermentation requires an Usp-type stress protein.

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    Authors
    Schreiber, Kerstin
    Boes, Nelli
    Eschbach, Martin
    Jaensch, Lothar
    Wehland, Juergen
    Bjarnsholt, Thomas
    Givskov, Michael
    Hentzer, Morten
    Schobert, Max
    Issue Date
    2006-01-01
    
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    Abstract
    Recently, we identified a pyruvate fermentation pathway in Pseudomonas aeruginosa sustaining anaerobic survival in the absence of alternative anaerobic respiratory and fermentative energy generation systems (M. Eschbach, K. Schreiber, K. Trunk, J. Buer, D. Jahn, and M. Schobert, J. Bacteriol. 186:4596-4604, 2004). Anaerobic long-term survival of P. aeruginosa might be essential for survival in deeper layers of a biofilm and the persistent infection of anaerobic mucus plaques in the cystic fibrosis lung. Proteome analysis of P. aeruginosa cells during a 7-day period of pyruvate fermentation revealed the induced synthesis of three enzymes involved in arginine fermentation, ArcA, ArcB, and ArcC, and the outer membrane protein OprL. Moreover, formation of two proteins of unknown function, PA3309 and PA4352, increased by factors of 72- and 22-fold, respectively. Both belong to the group of universal stress proteins (Usp). Long-term survival of a PA3309 knockout mutant by pyruvate fermentation was found drastically reduced. The oxygen-sensing regulator Anr controls expression of the PPA3309-lacZ reporter gene fusion after a shift to anaerobic conditions and further pyruvate fermentation. PA3309 expression was also found induced during the anaerobic and aerobic stationary phases. This aerobic stationary-phase induction is independent of the regulatory proteins Anr, RpoS, RelA, GacA, RhlR, and LasR, indicating a currently unknown mechanism of stationary-phase-dependent gene activation. PA3309 promoter activity was detected in the deeper layers of a P. aeruginosa biofilm using a PPA3309-gfp (green fluorescent protein gene) fusion and confocal laser-scanning microscopy. This is the first description of an Anr-dependent, anaerobically induced, and functional Usp-like protein in bacteria.
    Citation
    J. Bacteriol. 2006, 188(2):659-68
    URI
    http://hdl.handle.net/10033/14593
    DOI
    10.1128/JB.188.2.659-668.2006
    PubMed ID
    16385055
    Type
    Article
    Language
    en
    ISSN
    0021-9193
    ae974a485f413a2113503eed53cd6c53
    10.1128/JB.188.2.659-668.2006
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    Publications of Dept. Cell Biology (ZB)

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