Molecular analysis of the glucose-specific phosphoenolpyruvate : sugar phosphotransferase system from Lactobacillus casei and its links with the control of sugar metabolism

Abstract

Lactobacillus caseitransports glucose preferentially by a mannose-class phosphoenolpyruvate : sugar phosphotransferase system (PTS). The genomic analysis ofL. caseiallowed the authors to find a gene cluster (manLMNO) encoding the IIAB (manL), IIC (manM) and IID (manN) proteins of a mannose-class PTS, and a putative 121 aa protein of unknown function (encoded bymanO), homologues of which are also present inmanclusters that encode glucose/mannose transporters in other Gram-positive bacteria. TheL. casei manoperon is constitutively expressed into amanLMNOmessenger, but an additionalmanOtranscript was also detected. Upstream of themanoperon, two genes (upsRandupsA) were found which encode proteins resembling a transcriptional regulator and a membrane protein, respectively. Disruption of eitherupsRorupsAdid not affectmanLMNOtranscription, and had no effect on glucose uptake. Cells carrying amanOdeletion transported glucose at a rate similar to that of the wild-type strain. By contrast, amanMdisruption resulted in cells unable to transport glucose by the PTS, thus confirming the functional role of themangenes. In addition, themanMmutant exhibited neither inducer exclusion of maltose nor glucose repression. This result confirms the need for glucose transport through the PTS to trigger these regulatory processes inL. casei.