This Article 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 Michel, V. Articles by Hebraud, M. Search for Related Content PubMed PubMed Citation Articles by Michel, V. Articles by Hebraud, M.

 Previous Article  |  Next Article 

J. Bacteriol., Dec 1997, 7331-7342, Vol 179, No. 23
Copyright © 1997, American Society for Microbiology

The cold shock response of the psychrotrophic bacterium Pseudomonas fragi involves four low-molecular-mass nucleic acid-binding proteins

V Michel, I Lehoux, G Depret, P Anglade, J Labadie and M Hebraud
Station de Recherches sur la Viande, Unite de Recherches de Microbiologie, Institut National de la Recherche Agronomique de Theix, Saint-Genes-Champanelle, France.

The psychrotrophic bacterium Pseudomonas fragi was subjected to cold shocks from 30 or 20 to 5 degrees C. The downshifts were followed by a lag phase before growth resumed at a characteristic 5 degrees C growth rate. The analysis of protein patterns by two-dimentional gel electrophoresis revealed overexpression of 25 or 17 proteins and underexpression of 12 proteins following the 30- or 20-to-5 degrees C shift, respectively. The two downshifts shared similar variations of synthesis of 20 proteins. The kinetic analysis distinguished the induced proteins into cold shock proteins (Csps), which were rapidly but transiently overexpressed, and cold acclimation proteins (Caps), which were more or less rapidly induced but still overexpressed several hours after the downshifts. Among the cold-induced proteins, four low- molecular-mass proteins, two of them previously characterized as Caps (CapA and CapB), and heat acclimation proteins (Haps) as well as heat shock proteins (Hsps) for the two others (TapA and TapB) displayed higher levels of induction. Partial amino acid sequences, obtained by microsequencing, were used to design primers to amplify by PCR the four genes and then determine their nucleotide sequences. A BamHI-EcoRI restriction fragment of 1.9 kb, containing the complete coding sequence for capB, was cloned and sequenced. The four peptides belong to the family of small nucleic acid-binding proteins as CspA, the major Escherichia coli Csp. They are likely to play a major role in the adaptative response of P. fragi to environmental temperature changes.

This article has been cited by other articles:

• Reva, O. N., Weinel, C., Weinel, M., Bohm, K., Stjepandic, D., Hoheisel, J. D., Tummler, B. (2006). Functional Genomics of Stress Response in Pseudomonas putida KT2440. J. Bacteriol. 188: 4079-4092 [Abstract] [Full Text]  
• Tendeng, C., Krin, E., Soutourina, O. A., Marin, A., Danchin, A., Bertin, P. N. (2003). A Novel H-NS-like Protein from an Antarctic Psychrophilic Bacterium Reveals a Crucial Role for the N-terminal Domain in Thermal Stability. J. Biol. Chem. 278: 18754-18760 [Abstract] [Full Text]  
• Rakotoarivonina, H., Jubelin, G., Hebraud, M., Gaillard-Martinie, B., Forano, E., Mosoni, P. (2002). Adhesion to cellulose of the Gram-positive bacterium Ruminococcus albus involves type IV pili. Microbiology 148: 1871-1880 [Abstract] [Full Text]  
• Duche, O., Tremoulet, F., Glaser, P., Labadie, J. (2002). Salt Stress Proteins Induced in Listeria monocytogenes. Appl. Environ. Microbiol. 68: 1491-1498 [Abstract] [Full Text]  
• Thomas, T., Cavicchioli, R. (2000). Effect of Temperature on Stability and Activity of Elongation Factor 2 Proteins from Antarctic and Thermophilic Methanogens. J. Bacteriol. 182: 1328-1332 [Abstract] [Full Text]