Effect of growth temperatures on the protein levels in a psychrotrophic bacterium, Pseudomonas fragi

Pseudomonas fragi has the ability to grow between 0 and 35 degrees C and grows optimally at 30 degrees C. Cellular proteins from mid-log-phase cells growing from 4 to 34 degrees C were labeled with L-[35S]methionine during 1 generation time and analyzed by two-dimensional gel electrophoresis. The electrophoretic patterns revealed differences in the patterns of protein synthesis over this temperature span. A qualitative comparison of cellular proteins led to their separation into five thermal classes. The first class contained proteins whose relative rates of synthesis were unaffected by the growth temperature. Three other classes included proteins with optimal expression at 4 to 10, 15 to 20, and 25 to 30 degrees C. A fifth class contained proteins which were more specifically synthesized at a supraoptimal growth temperature (34 degrees C). Two low-molecular-mass proteins, designated C7.0 and C8.0, were highly concentrated at 4 to 10 degrees C, and their relative rates of synthesis steadily increased with decreasing temperature. Polyclonal antibodies were separately raised against these two proteins. Immunological analyses revealed cross-reaction between these two proteins and between two additional low-molecular-mass proteins which were maximally produced at elevated temperatures. Antisera directed against C8.0 recognized the major cold shock protein of Escherichia coli, CspA, indicating the presence of similarities between these proteins.

[1]  C. Debouck,et al.  Identification and characterization of novel low-temperature-inducible promoters of Escherichia coli , 1992, Journal of bacteriology.

[2]  L. Whyte,et al.  Cold shock proteins and cold acclimation proteins in a psychrotrophic bacterium , 1992 .

[3]  Y. Av‐Gay,et al.  Streptomyces contain a 7.0 kDa cold shock like protein. , 1992, Nucleic acids research.

[4]  M. Marahiel,et al.  Characterization of cspB, a Bacillus subtilis inducible cold shock gene affecting cell viability at low temperatures , 1992, Journal of bacteriology.

[5]  A. Wolffe,et al.  DNA gyrase, CS7.4, and the cold shock response in Escherichia coli , 1992, Journal of bacteriology.

[6]  F. Neidhardt,et al.  Function of a relaxed-like state following temperature downshifts in Escherichia coli , 1992, Journal of bacteriology.

[7]  A. Wolffe,et al.  The Y-box factors: a family of nucleic acid binding proteins conserved from Escherichia coli to man. , 1992, The New biologist.

[8]  C. Gualerzi,et al.  Identification of a cold shock transcriptional enhancer of the Escherichia coli gene encoding nucleoid protein H-NS. , 1991, Proceedings of the National Academy of Sciences of the United States of America.

[9]  T. Araki Changes in rates of synthesis of individual proteins in a psychrophilic bacterium after a shift in temperature. , 1991, Canadian journal of microbiology.

[10]  A. Gounot Bacterial life at low temperature: physiological aspects and biotechnological implications. , 1991, The Journal of applied bacteriology.

[11]  N. Orange,et al.  Effect of growth temperature on several exported enzyme activities in the psychrotrophic bacterium Pseudomonas fluorescens , 1991, Journal of bacteriology.

[12]  T. Araki The effect of temperature shifts on protein synthesis by the psychrophilic bacterium Vibrio sp. strain ANT-300. , 1991, Journal of general microbiology.

[13]  D. Friedman,et al.  Identification of a second promoter for the metY-nusA-infB operon of Escherichia coli , 1990, Journal of bacteriology.

[14]  A. Hipkiss,et al.  Temperature-dependent changes in proteolytic activities and protein composition in the psychrotrophic bacterium Arthrobacter globiformis S155 , 1990 .

[15]  N J Russell,et al.  Cold adaptation of microorganisms. , 1990, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.

[16]  R. Jaenicke Protein structure and function at low temperatures. , 1990, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.

[17]  M. Grunberg‐Manago,et al.  Nucleotide sequence of the pnp gene of Escherichia coli encoding polynucleotide phosphorylase. Homology of the primary structure of the protein with the RNA-binding domain of ribosomal protein S1. , 1987, The Journal of biological chemistry.

[18]  D. Fairbairn,et al.  Proteinases of psychrotrophic bacteria: their production, properties, effects and control , 1986, Journal of Dairy Research.

[19]  R. Mckellar Factors influencing the production of extracellular proteinase by Pseudomonas fluorescens. , 1982, The Journal of applied bacteriology.

[20]  F. Neidhardt,et al.  Levels of major proteins of Escherichia coli during growth at different temperatures , 1979, Journal of bacteriology.

[21]  D. Pope,et al.  Effects of low temperature on in vivo and in vitro protein synthesis in Escherichia coli and Pseudomonas fluorescens , 1978, Journal of bacteriology.

[22]  M. M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. , 1976, Analytical biochemistry.

[23]  R. Y. Morita,et al.  PSYCHROPHILIC BACTERIA , 1959, Bacteriological reviews.

[24]  P. O’Farrell High resolution two-dimensional electrophoresis of proteins. , 1975, The Journal of biological chemistry.

[25]  U. K. Laemmli,et al.  Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.

[26]  W. Szer Cell-free protein synthesis at 0°: An activating factor from ribosomes of a psychrophilic microorganism , 1970 .

[27]  F. Neidhardt,et al.  The gene‐protein database of Escherichia coli: Edition 5 , 1992, Electrophoresis.

[28]  F. Neidhardt,et al.  The gene‐protein database of Escherichia coli: Edition 4 , 1991, Electrophoresis.

[29]  M. Inouye,et al.  Major cold shock protein of Escherichia coli. , 1990, Proceedings of the National Academy of Sciences of the United States of America.

[30]  N. Fukunaga,et al.  Effect of temperature on natural mRNA-directed protein synthesis in psychrophilic and mesophilic bacteria , 1987 .

[31]  Roberts Ta,et al.  Microbial and chemical changes in chill-stored red meats. , 1983 .

[32]  T. A. Roberts,et al.  Microbial and chemical changes in chill-stored red meats. , 1983, Society for Applied Bacteriology symposium series.

[33]  R. Rosset Chilling, Freezing and Thawing , 1982 .

[34]  T. Horii,et al.  Organization of the recA gene of Escherichia coli. , 1980, Proceedings of the National Academy of Sciences of the United States of America.

[35]  N. Fukunaga,et al.  EFFECT OF TEMPERATURE ON THE CELL-FREE PROTEIN-SYNTHESIZING SYSTEM IN PSYCHROPHILIC AND MESOPHILIC BACTERIA , 1980 .