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Microbiology and Molecular Biology Reviews, December 2006, p. 939-1031, Vol. 70, No. 4
1092-2172/06/$08.00+0     doi:10.1128/MMBR.00024-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria{dagger}

Josef Deutscher,1* Christof Francke,2 and Pieter W. Postma3

Microbiologie et Génétique Moléculaire, INRA-CNRS-INA PG UMR 2585, Thiverval-Grignon, France,1 Department of Molecular Cell Physiology, Biocentrum, Vrije Universiteit, Amsterdam, and Wageningen Centre for Food Sciences at CMBI, Radboud University, Nijmegen, The Netherlands,2 Swammerdam Institute for Life Sciences, BioCentrum, University of Amsterdam, Amsterdam, The Netherlands3

The phosphoenolpyruvate(PEP):carbohydrate phosphotransferase system (PTS) is found only in bacteria, where it catalyzes the transport and phosphorylation of numerous monosaccharides, disaccharides, amino sugars, polyols, and other sugar derivatives. To carry out its catalytic function in sugar transport and phosphorylation, the PTS uses PEP as an energy source and phosphoryl donor. The phosphoryl group of PEP is usually transferred via four distinct proteins (domains) to the transported sugar bound to the respective membrane component(s) (EIIC and EIID) of the PTS. The organization of the PTS as a four-step phosphoryl transfer system, in which all P derivatives exhibit similar energy (phosphorylation occurs at histidyl or cysteyl residues), is surprising, as a single protein (or domain) coupling energy transfer and sugar phosphorylation would be sufficient for PTS function. A possible explanation for the complexity of the PTS was provided by the discovery that the PTS also carries out numerous regulatory functions. Depending on their phosphorylation state, the four proteins (domains) forming the PTS phosphorylation cascade (EI, HPr, EIIA, and EIIB) can phosphorylate or interact with numerous non-PTS proteins and thereby regulate their activity. In addition, in certain bacteria, one of the PTS components (HPr) is phosphorylated by ATP at a seryl residue, which increases the complexity of PTS-mediated regulation. In this review, we try to summarize the known protein phosphorylation-related regulatory functions of the PTS. As we shall see, the PTS regulation network not only controls carbohydrate uptake and metabolism but also interferes with the utilization of nitrogen and phosphorus and the virulence of certain pathogens.

* Corresponding author. Mailing address: Laboratoire de Microbiologie et Génétique Moléculaire, CNRS/INRA/INA-PG UMR2585, F-78850 Thiverval-Grignon, France. Phone: 33-1-30815447. Fax: 33-1-30815457. E-mail: Josef.Deutscher{at}grignon.inra.fr.

{dagger} Pieter W. Postma passed away during the preparation of this review. The loss that we experienced has been put into words by Gary R. Jacobson and Joseph W. Lengeler (368).

Microbiology and Molecular Biology Reviews, December 2006, p. 939-1031, Vol. 70, No. 4
1092-2172/06/$08.00+0     doi:10.1128/MMBR.00024-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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