Journal
EUROPEAN JOURNAL OF CELL BIOLOGY
Volume 90, Issue 9, Pages 711-720Publisher
ELSEVIER GMBH, URBAN & FISCHER VERLAG
DOI: 10.1016/j.ejcb.2011.04.002
Keywords
Bacterial phosphotransferase system; PIS; Glucose; Carbohydrate transport; Integral membrane protein; Gene regulation; Catabolite repression; Metabolic balance; Modeling; ptsG; Mlc; MtfA; SgrT
Categories
Funding
- German Research Foundation [SFB421]
- German Federal Ministry of Education and Research (BMBF) [FKZ0315285A, FKZ0315285C]
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The phosphoenolpyruvate-(PEP)-dependent-carbohydrate:phosphotransferase systems (PTSs) of enteric bacteria constitute a complex transport and sensory system. Such a PTS usually consists of two cytoplasmic energy-coupling proteins, Enzyme I (El) and HPr, and one of more than 20 different carbohydrate-specific membrane proteins named Enzyme II (Ell), which catalyze the uptake and concomitant phosphorylation of numerous carbohydrates. The most prominent representative is the glucose-PTS, which uses a PTS-typical phosphcrylation cascade to transport and phosphorylate glucose. All components of the glucose-PTS interact with a large number of non-PTS proteins to regulate the carbohydrate flux in the bacterial cell. Several aspects of the glucose-PTS have been intensively investigated in various research projects of many groups. In this article we will review our recent findings on a Glc-PTS-dependent metalloprotease, on the interaction of EIICBGlc with the regulatory peptide SgrT, on the structure of the membrane spanning C-domain of the glucose transporter and on the modeling approaches of ptsG regulation, respectively, and discuss them in context of general PTS research. (C) 2011 Elsevier GmbH. All rights reserved.
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