title: Glycerol metabolism and PrfA activity in Listeria monocytogenes.
abstract: Listeria monocytogenes is able to efficiently utilize glycerol as a carbon source. In a defined minimal medium, the growth rate (during balanced growth) in the presence of glycerol is similar to that in the presence of glucose or cellobiose. Comparative transcriptome analyses of L. monocytogenes showed high-level transcriptional upregulation of the genes known to be involved in glycerol uptake and metabolism (glpFK and glpD) in the presence of glycerol (compared to that in the presence of glucose and/or cellobiose). Levels of expression of the genes encoding a second putative glycerol uptake facilitator (GlpF(2)) and a second putative glycerol kinase (GlpK(2)) were less enhanced under these conditions. GlpK(1) but not GlpK(2) was essential for glycerol catabolism in L. monocytogenes under extracellular conditions, while the loss of GlpK(1) affected replication in Caco-2 cells less than did the loss of GlpK(2) and GlpD. Additional genes whose transcription levels were higher in the presence of glycerol than in the presence of glucose and cellobiose included those for two dihydroxyacetone (Dha) kinases and many genes that are under carbon catabolite repression control. Transcriptional downregulation in the presence of glycerol (compared to those in the presence glucose and cellobiose) was observed for several genes and operons that are positively regulated by glucose, including genes involved in glycolysis, N metabolism, and the biosynthesis of branched-chain amino acids. The highest level of transcriptional upregulation was observed for all PrfA-dependent genes during early and late logarithmic growth in glycerol. Under these conditions, a low level of HPr-Ser-P and a high level of HPr-His-P were present in the cells, suggesting that all enzyme IIA (EIIA) (or EIIB) components of the phosphotransferase system (PTS) permeases expressed will be phosphorylated. These and other data suggest that the phosphorylation state of PTS permeases correlates with PrfA activity.
authors.affiliation: Institut für Hygiene und Mikrobiologie, Universität Würzburg, Gebäude E1, 97080 Würzburg, Germany. bjoseph@hygiene.uni-wuerzburg.de
authors.forename: Biju
authors.initials: B
authors.lastname: Joseph
authors.forename: Sonja
authors.initials: S
authors.lastname: Mertins
authors.forename: Regina
authors.initials: R
authors.lastname: Stoll
authors.forename: Jennifer
authors.initials: J
authors.lastname: Schär
authors.forename: Kanasinakatte Rudrappa
authors.initials: KR
authors.lastname: Umesha
authors.forename: Qin
authors.initials: Q
authors.lastname: Luo
authors.forename: Stefanie
authors.initials: S
authors.lastname: Müller-Altrock
authors.forename: Werner
authors.initials: W
authors.lastname: Goebel
mesh_terms: D000818:Animals; D001426:Bacterial Proteins / Q000096:biosynthesis / Q000235:genetics; D002460:Cell Line; D002475:Cellobiose / Q000378:metabolism; D015536:Down-Regulation; D004847:Epithelial Cells / Q000382:microbiology; D017353:Gene Deletion; D020869:Gene Expression Profiling; D005816:Genetic Complementation Test; D005947:Glucose / Q000378:metabolism; D005990:Glycerol / Q000378:metabolism*; D006801:Humans; D008089:Listeria monocytogenes / Q000378:metabolism / Q000472:pathogenicity / Q000502:physiology*; D008264:Macrophages / Q000382:microbiology; D026901:Membrane Transport Proteins / Q000378:metabolism; D051379:Mice; D020411:Oligonucleotide Array Sequence Analysis; D010454:Peptide Termination Factors / Q000378:metabolism*; D010766:Phosphorylation; D015854:Up-Regulation
chemical_list: D001426:Bacterial Proteins; D026901:Membrane Transport Proteins; D010454:Peptide Termination Factors; D002475:Cellobiose; D005947:Glucose; D005990:Glycerol