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Department of Biology, University of California at San Diego, La Jolla, CA 92093-0116, USA
* Author for correspondence: Milton H. Saier, Jr. Tel: +1 619 534 4084. Fax: +1 619 534 7108. e-mail: msaier@ucsd.edu
ABSTRACT
Inducer expulsion, a phenomenon in which rapidly metabolizable sugars cause cytoplasmic dephosphorylation and efflux of pre-accumulated sugar-phosphates (sugar-P), has been documented for Streptococcus pyogenes, Streptococcus bovis and Lactococcus lactis but not for other Gram-positive bacteria. Using intact cells and membrane vesicles, we show that Enterococcus faecalis exhibits both inducer exclusion and inducer expulsion, and that the latter phenomenon is dependent on the metabolite-activated ATP-dependent HPr(Ser) kinase that phosphorylates Ser-46 in HPr of the phosphotransferase system. A small, heat-stable, membrane-associated, HPr(Ser-P)-activated sugar-P phosphatase (Pase II), previously identified only in Lc. lactis is shown to be present in extracts of Enterococcus faecalis and Streptococcus pyogenes but not in those of Staphylococcus aureus, Streptococcus mutans, Streptococcus salivarius or Bacillis subtilis organisms that do not exhibit the inducer expulsion phenomenon. Further, Lactobacillus brevis an organism that exhibits inducer expulsion by a different mechanism, also apparently lacks Pase II. The results reveal that Pase II is present in those organisms that exhibit the coupled sugar-P hydrolysis/expulsion mechanism but not those that lack this mechanism. They provide correlative evidence that Pase II initiates inducer expulsion in species of enterococci, streptococci and lactococci.
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