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J Bacteriol. 1971 July; 107(1): 223-229
Copyright © 1971 American Society for Microbiology. All Rights Reserved.
a Departments of Microbiology and Biochemistry, Scripps Clinic and Research Foundation, La Jolla, California 92037, and Department of Microbiology, University of Rochester, Rochester, New York 14620
ABSTRACT
Polyglycerolteichoic acid:glucosyl transferase (TAG transferase), one of the three enzymes involved in the pathway leading to the glucosylation of teichoic acid in Bacillus subtilis 168, was investigated. During the early stages of the growth of B. subtilis, TAG transferase is predominantly a soluble enzyme found in the cytoplasm. As growth proceeds, the amount of soluble enzyme decreases and the proportion of insoluble, membrane-bound TAG transferase increases, reaching a maximal value at the close of the logarithmic phase. Data are presented which suggest that these are two forms of the same enzyme, or have some common component. The effects of chaotropic agents, such as sodium trichloroacetate and sodium perchlorate, on the cytoplasmic membrane were also studied. These data show that such compounds can effectively remove the TAG transferase from the membrane in a water-soluble form. A study of some of the physical properties of this solubilized enzyme suggests that there is little difference between the two forms of the enzyme. Experiments are described which indicate that the glucosyl transfer by both the membrane-bound and soluble enzymes is not mediated by lipids.
2 Present address: Department of Microbiology, School of Medicine and Dentistry, University of Rochester, Rochester, N.Y. 14620.
3 Present address: Department of Microbiology, University of Colorado, Denver, Colo.
1 A preliminary report of this work was presented at the 10th International Congress for Microbiology, Mexico City, Mexico, 9-15 August 1970.
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