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Extracellular Enzyme Secretion by Pseudomonas lemoignei

¹ Department of Microbiology, School of Medicine, State University of New York at Buffalo, Buffalo, New York 14214

ABSTRACT

The ability of succinate to repress the secretion of Pseudomonas lemoignei poly-ß-hydroxybutyrate depolymerase was a function of pH. Repression only occurred when the pH of the medium was 7.0 or less. At a higher pH, lack of sensitivity to succinate concentration may have been due to a limited ability to transport succinate. Actively secreting cultures (at pH 7.4) continued to secrete enzyme for approximately 30 min after the pH was rapidly decreased to pH 6.8, even though sufficient succinate was present to repress enzyme synthesis. Similarly, after the addition of rifampin to secreting cultures, there was a 30-min delay before secretion was inhibited. Evidence is presented which suggests that continued secretion may be the result of depolymerase messenger ribonucleic acid accumulation within the cells. Studies with chloramphenicol indicated that de novo protein synthesis is necessary for the secretion of poly-ß-hydroxybutyrate depolymerase and that exoenzyme is not released from a preformed pool. Studies with various inhibitors of protein synthesis indicated that synthesis of exoenzyme is 5 to 10 times more susceptible to inhibition than is the synthesis of cell-associated proteins.

This article has been cited by other articles:

• Terpe, K., Kerkhoff, K., Pluta, E., Jendrossek, D. (1999). Relationship between Succinate Transport and Production of Extracellular Poly(3-Hydroxybutyrate) Depolymerase in Pseudomonas lemoignei. Appl. Environ. Microbiol. 65: 1703-1709 [Abstract] [Full Text]  
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