This Article Full Text Full Text (PDF) Supplemental material Other Versions of this Article: JB.00259-08v1 190/15/5412    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Google Scholar Articles by Joseph, B. Articles by Goebel, W. PubMed PubMed Citation Articles by Joseph, B. Articles by Goebel, W.

 Previous Article  |  Next Article 

Journal of Bacteriology, August 2008, p. 5412-5430, Vol. 190, No. 15
0021-9193/08/$08.00+0     doi:10.1128/JB.00259-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Glycerol Metabolism and PrfA Activity in Listeria monocytogenes ^,

Biju Joseph,^* Sonja Mertins,^, Regina Stoll, Jennifer Schär, Kanasinakatte Rudrappa Umesha,^¶ Qin Luo,^|| Stefanie Müller-Altrock, and Werner Goebel

Lehrstuhl für Mikrobiologie, Biozentrum, Universität Würzburg, D-97074 Würzburg, Germany

Received 20 February 2008/ Accepted 20 May 2008

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 (GlpF₂) and a second putative glycerol kinase (GlpK₂) were less enhanced under these conditions. GlpK₁ but not GlpK₂ was essential for glycerol catabolism in L. monocytogenes under extracellular conditions, while the loss of GlpK₁ affected replication in Caco-2 cells less than did the loss of GlpK₂ 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.

Published ahead of print on 23 May 2008.

Supplemental material for this article may be found at http://jb.asm.org/.

B.J. and S.M. contributed equally to this work.

Present address: Vaccine and Infectious Disease Organization, 120 Veterinary Road, Saskatoon, Saskatchewan S7N 5E3, Canada.

^¶ Present address: Department of Fishery Microbiology, Karnataka Veterinary, Animal and Fisheries Sciences University, College of Fisheries, Mangalore 575 002, India.

^|| Present address: College of Life Science, Central China Normal University, Wuhan 430079, China.