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Journal of Bacteriology, April 2004, p. 2385-2392, Vol. 186, No. 8
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.8.2385-2392.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Identification of a Phosphotransferase System of Escherichia coli Required for Growth on N-Acetylmuramic Acid

Ulrike Dahl, Tina Jaeger, Bao Trâm Nguyen, Julia M. Sattler, and Christoph Mayer*

Fachbereich Biologie, University of Konstanz, 78457 Konstanz, Germany

Received 12 November 2003/ Accepted 6 January 2004

We report here that wild-type Escherichia coli grows on N-acetylmuramic acid (MurNAc) as the sole source of carbon and energy. Analysis of mutants defective in N-acetylglucosamine (GlcNAc) catabolism revealed that the catabolic pathway for MurNAc merges into the GlcNAc pathway on the level of GlcNAc 6-phosphate. Furthermore, analysis of mutants defective in components of the phosphotransferase system (PTS) revealed that a PTS is essential for growth on MurNAc. However, neither the glucose-, mannose/glucosamine-, nor GlcNAc-specific PTS (PtsG, ManXYZ, and NagE, respectively) was found to be necessary. Instead, we identified a gene at 55 min on the E. coli chromosome that is responsible for MurNAc uptake and growth. It encodes a single polypeptide consisting of the EIIB and C domains of a so-far-uncharacterized PTS that was named murP. MurP lacks an EIIA domain and was found to require the activity of the crr-encoded enzyme IIA-glucose (EIIAGlc), a component of the major glucose transport system for growth on MurNAc. murP deletion mutants were unable to grow on MurNAc as the sole source of carbon; however, growth was rescued by providing murP in trans expressed from an isopropylthiogalactopyranoside-inducible plasmid. A functional His6 fusion of MurP was constructed, isolated from membranes, and identified as a polypeptide with an apparent molecular mass of 37 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blot analysis. Close homologs of MurP were identified in the genome of several bacteria, and we believe that these organisms might also be able to utilize MurNAc.

* Corresponding author. Mailing address: Fachbereich Biologie, Universität Konstanz, Universitätsstr. 10, 78457 Konstanz, Germany. Phone: (49) 7531 884854. Fax: (49) 7531 883356. E-mail: ch.mayer{at}uni-konstanz.de.

Journal of Bacteriology, April 2004, p. 2385-2392, Vol. 186, No. 8
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.8.2385-2392.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Jaeger, T., Mayer, C. (2008). The Transcriptional Factors MurR and Catabolite Activator Protein Regulate N-Acetylmuramic Acid Catabolism in Escherichia coli. J. Bacteriol. 190: 6598-6608 [Abstract] [Full Text]  
  • Park, J. T., Uehara, T. (2008). How Bacteria Consume Their Own Exoskeletons (Turnover and Recycling of Cell Wall Peptidoglycan). Microbiol. Mol. Biol. Rev. 72: 211-227 [Abstract] [Full Text]  
  • Uehara, T., Suefuji, K., Jaeger, T., Mayer, C., Park, J. T. (2006). MurQ Etherase Is Required by Escherichia coli in Order To Metabolize Anhydro-N-Acetylmuramic Acid Obtained either from the Environment or from Its Own Cell Wall. J. Bacteriol. 188: 1660-1662 [Abstract] [Full Text]  
  • Jaeger, T., Arsic, M., Mayer, C. (2005). Scission of the Lactyl Ether Bond of N-Acetylmuramic Acid by Escherichia coli "Etherase". J. Biol. Chem. 280: 30100-30106 [Abstract] [Full Text]  
  • Uehara, T., Suefuji, K., Valbuena, N., Meehan, B., Donegan, M., Park, J. T. (2005). Recycling of the Anhydro-N-Acetylmuramic Acid Derived from Cell Wall Murein Involves a Two-Step Conversion to N-Acetylglucosamine-Phosphate. J. Bacteriol. 187: 3643-3649 [Abstract] [Full Text]  


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