Physiological consequences of starvation in Pseudomonas putida: degradation of intracellular protein and loss of activity of the inducible enzymes of L-arginine catabolism.

Journal of Bacteriology
C L Fan, V W Rodwell

Abstract

We investigated the degradation of radioisotopically labeled intracellular protein in starved, intact cells of Pseudomonas putida P2 (ATCC 25571) and the regulation of this process. Intracellular protein isotopically labeled with L-[4,5-3H]leucine during log-phase growth at 30 C is degraded at rates of 1 to 2%/h in log-phase cells and 7 to 9%/h in starved cells. Rifampin, chloramphenicol, and tosyllysine chloromethylketone lower the rate of protein degradation by starved cells. Addition to starved cells of a nutrient upon which the culture is induced for growth rapidly lowers the rate of protein degradation from 7 to 9%/h to less than 1.5%/h. A nutrient that is oxidized but that cannot immediately support growth also lowers the rate of starvation-induced protein degradation. Proteolytic activity of cell extracts requires a divalent metal ion and may be inhibited up to 60% by tosyllysine chloromethylketone or p-toluenesulfonyl fluoride. Rifampin and chloramphenicol have no effect. In contrast to intact cells, extracts of growing or starving cells degrade protein at equivalent rates. We also investigated the stabilities of the inducible transport system and of four inducible intracellular enzymes of L-arginine catabolism. These i...Continue Reading

References

Apr 16, 1971·Biochemical and Biophysical Research Communications·J S Bond
Jan 1, 1972·Annual Review of Microbiology·M J Pine
Jul 8, 1965·Biochimica Et Biophysica Acta·M J Pine
May 1, 1967·The Biochemical Journal·N S Willetts
Jun 1, 1964·Proceedings of the National Academy of Sciences of the United States of America·P B SIGLERD R DAVIES

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Citations

Jul 1, 1989·Biotechnology and Bioengineering·S F Karel, C R Robertson
Mar 1, 1980·Journal of Bacteriology·N B Wood, R Haselkorn
Jan 1, 1983·Molecular and Biochemical Parasitology·M W Simon, A J Mukkada

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