This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Jaouen, T. Articles by Orange, N. Search for Related Content PubMed PubMed Citation Articles by Jaouen, T. Articles by Orange, N. Agricola Articles by Jaouen, T. Articles by Orange, N.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, November 2004, p. 6665-6669, Vol. 70, No. 11
0099-2240/04/$08.00+0     DOI: 10.1128/AEM.70.11.6665-6669.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Pore Size Dependence on Growth Temperature Is a Common Characteristic of the Major Outer Membrane Protein OprF in Psychrotrophic and Mesophilic Pseudomonas Species

Thomas Jaouen,¹ Emmanuelle Dé,² Sylvie Chevalier,¹ and Nicole Orange^1*

Laboratoire de Microbiologie du Froid, UPRES 2123, Université de Rouen, Evreux,¹ Institut Fédératif de Recherche Multidisciplinaire sur les Peptides, UMR 6522, CNRS, Université de Rouen, Mont Saint Aignan, France²

Received 8 March 2004/ Accepted 23 June 2004

Pseudomonas species adapt well to hostile environments, which are often subjected to rapid variations. In these bacteria, the outer membrane plays an important role in the sensing of environmental conditions such as temperature. In previous studies, it has been shown that in the psychrotrophic strain P. fluorescens MF0, the major porin OprF changes its channel size according to the growth conditions and could affect outer membrane permeability. Studies of the channel-forming properties of OprFs from P. putida 01G3 and P. aeruginosa PAO1 in planar lipid bilayers generated similar results. The presence of a cysteine- or proline-rich cluster in the central linker region is not essential for channel size modulations. These findings suggest that OprF could adopt two alternative conformations in the outer membrane and that folding is thermoregulated. In contrast, no difference according to growth temperature was observed for structurally different outer membrane proteins, such as OprE3 from the Pseudomonas OprD family of specific porins. Our results are consistent with the fact that the decrease in channel size observed at low growth temperature is a particular feature of the OprF porin in various psychrotrophic and mesophilic Pseudomonas species isolated from diverse ecological niches. The ability to reduce outer membrane permeability at low growth temperature could provide these bacteria with adaptive advantages.

---

* Corresponding author. Mailing address: Laboratoire de Microbiologie du Froid, UPRES 2123, Université de Rouen, 55 rue Saint Germain, 27000 Evreux, France. Phone: 33.02.32.29.15.66. Fax: 33.02.32.29.15.66. E-mail: nicole.orange{at}univ-rouen.fr.

---

Applied and Environmental Microbiology, November 2004, p. 6665-6669, Vol. 70, No. 11
0099-2240/04/$08.00+0     DOI: 10.1128/AEM.70.11.6665-6669.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

This article has been cited by other articles:

• Sugawara, E., Nestorovich, E. M., Bezrukov, S. M., Nikaido, H. (2006). Pseudomonas aeruginosa Porin OprF Exists in Two Different Conformations. J. Biol. Chem. 281: 16220-16229 [Abstract] [Full Text]  
• Bodilis, J., Barray, S. (2006). Molecular evolution of the major outer-membrane protein gene (oprF) of Pseudomonas.. Microbiology 152: 1075-1088 [Abstract] [Full Text]