The phosphoenolpyruvate-dependent glucose-phosphotransferase system from Escherichia coli K-12 as the center of a network regulating carbohydrate flux in the cell

DC FieldValueLanguage
dc.contributor.authorGabor, Elisabeth
dc.contributor.authorGoehler, Anna-Katharina
dc.contributor.authorKosfeld, Anne
dc.contributor.authorStaab, Ariane
dc.contributor.authorKremling, Andreas
dc.contributor.authorJahreis, Knut
dc.date.accessioned2021-12-23T16:09:28Z-
dc.date.available2021-12-23T16:09:28Z-
dc.date.issued2011
dc.identifier.issn01719335
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/8817-
dc.description.abstractThe 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.
dc.description.sponsorshipGerman Research FoundationGerman Research Foundation (DFG) [SFB421]; German Federal Ministry of Education and Research (BMBF)Federal Ministry of Education & Research (BMBF) [FKZ0315285A, FKZ0315285C]; We would like to thank Kurt Schmid, Fritz Titgemeyer, Katja Bettenbrock and Jurgen Heinisch for helpful discussions, the many students, who helped with this project, Katrin Fanger for technical assistance, Lucille Schmieding for help with the manuscript, the German Research Foundation for financial support (SFB421, project P14) and the German Federal Ministry of Education and Research (BMBF, grant FKZ0315285A and FKZ0315285C). We dedicate this review to Joseph W. Lengeler, a great PTS scientist, who retired in the year 2002.
dc.language.isoen
dc.publisherELSEVIER GMBH, URBAN & FISCHER VERLAG
dc.relation.ispartofEUROPEAN JOURNAL OF CELL BIOLOGY
dc.subjectBacterial phosphotransferase system
dc.subjectCarbohydrate transport
dc.subjectCATABOLITE REPRESSION
dc.subjectCell Biology
dc.subjectCYSTEINE CROSS-LINKING
dc.subjectGene regulation
dc.subjectGLOBAL REPRESSOR MLC
dc.subjectGlucose
dc.subjectIntegral membrane protein
dc.subjectMANNITOL PERMEASE
dc.subjectMEMBRANE SEQUESTRATION
dc.subjectMetabolic balance
dc.subjectMlc
dc.subjectModeling
dc.subjectMtfA
dc.subjectPIS
dc.subjectPOSTTRANSCRIPTIONAL REGULATION
dc.subjectptsG
dc.subjectSgrT
dc.subjectSIGNAL-TRANSDUCTION
dc.subjectSUBSTRATE-SPECIFICITY
dc.subjectTRANSPORTER MESSENGER-RNA
dc.subjectUNCOUPLE TRANSPORT
dc.titleThe phosphoenolpyruvate-dependent glucose-phosphotransferase system from Escherichia coli K-12 as the center of a network regulating carbohydrate flux in the cell
dc.typereview
dc.identifier.doi10.1016/j.ejcb.2011.04.002
dc.identifier.isiISI:000295199600005
dc.description.volume90
dc.description.issue9
dc.description.startpage711
dc.description.endpage720
dc.identifier.eissn16181298
dc.publisher.placeOFFICE JENA, P O BOX 100537, 07705 JENA, GERMANY
dcterms.isPartOf.abbreviationEur. J. Cell Biol.
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