[Advances in mechanism of Escherichia coli carbon catabolite repression].

Bacteria often sequentially utilize coexisting carbohydrates in environment and firstly select the one (frequently glucose) easiest to metabolize. This phenomenon is known as carbon catabolite repression (CCR). In existing Chinese teaching materials of molecular biology and related courses, unclear or even wrong interpretations are given about CCR mechanism. A large number of studies have shown that rather than the existence of intracellular glucose, CCR is mainly caused by the glucose transport process coupling with glucose phosphorylation via the phosphoenolpyruvate: carbohydrate phosphotransferase system PTS. The transport process leads to accumulation of dephosphorylated form of EAGlc.This form of EAGlc can bind the membrane-localized LacY protein to block the uptake of lactose inducer. cAMP functions in activation of key genes involved in PTS system to strengthen the role of inducer exclusion. In addition, dephosphorylated form of EBGlc and Yee bind global transcription repressor Mlc to ensure the expression of key genes involved in the PTS system. This review summarizes the current advancement in mechanism of Escherichia coli carbon catabolite repression.

[1]  A. Narang.  cAMP does not have an important role in carbon catabolite repression of the Escherichia coli lac operon , 2009, Nature Reviews Microbiology.

[2]  B. Görke,et al.  Is there any role for cAMP–CRP in carbon catabolite repression of the Escherichia coli lac operon? Reply from Görke and Stülke , 2008, Nature Reviews Microbiology.

[3]  M. Crasnier-Mednansky.  Is there any role for cAMP–CRP in carbon catabolite repression of the Escherichia coli lac operon? , 2008, Nature Reviews Microbiology.

[4]  B. Görke,et al.  Carbon catabolite repression in bacteria: many ways to make the most out of nutrients , 2008, Nature Reviews Microbiology.

[5]  J. Deutscher,et al.  The mechanisms of carbon catabolite repression in bacteria. , 2008, Current opinion in microbiology.

[6]  Andreas Kremling,et al.  Correlation between Growth Rates, EIIACrr Phosphorylation, and Intracellular Cyclic AMP Levels in Escherichia coli K-12 , 2007, Journal of bacteriology.

[7]  C. Francke,et al.  How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria , 2006, Microbiology and Molecular Biology Reviews.

[8]  Winfried Boos,et al.  YeeI, a Novel Protein Involved in Modulation of the Activity of the Glucose-Phosphotransferase System in Escherichia coli K-12 , 2006, Journal of bacteriology.

[9]  Y. Seok,et al.  In Vitro Reconstitution of Catabolite Repression in Escherichia coli* , 2006, Journal of Biological Chemistry.

[10]  Guillermo Gosset,et al.  Improvement of Escherichia coli production strains by modification of the phosphoenolpyruvate:sugar phosphotransferase system , 2005, Microbial cell factories.

[11]  H. Aiba,et al.  Membrane localization itself but not binding to IICBGlc is directly responsible for the inactivation of the global repressor Mlc in Escherichia coli , 2004, Molecular microbiology.

[12]  W. Boos,et al.  Analysis of the Interaction between the Global Regulator Mlc and EIIBGlc of the Glucose-specific Phosphotransferase System in Escherichia coli * , 2003, The Journal of Biological Chemistry.

[13]  J. Plumbridge,et al.  Regulation of gene expression in the PTS in Escherichia coli: the role and interactions of Mlc. , 2002, Current opinion in microbiology.

[14]  J. Sun,et al.  Deduction of consensus binding sequences on proteins that bind IIAGlc of the phosphoenolpyruvate:sugar phosphotransferase system by cysteine scanning mutagenesis of Escherichia coli lactose permease. , 1999, Proceedings of the National Academy of Sciences of the United States of America.

[15]  P. Postma,et al.  cAMP receptor protein-cAMP plays a crucial role in glucose-lactose diauxie by activating the major glucose transporter gene in Escherichia coli. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[16]  T. Inada,et al.  Mechanism responsible for glucose–lactose diauxie in Escherichia coli: challenge to the cAMP model , 1996, Genes to cells : devoted to molecular & cellular mechanisms.

[17]  J. Rosenbusch,et al.  Cysteine phosphorylation of the glucose transporter of Escherichia coli. , 1993, The Journal of biological chemistry.

[18]  G R Jacobson,et al.  Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria. , 1993, Microbiological reviews.

[19]  A Danchin,et al.  The ptsH, ptsI, and crr genes of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system: a complex operon with several modes of transcription , 1988, Journal of bacteriology.

[20]  T. Doering,et al.  Sugar transport by the bacterial phosphotransferase system. Molecular cloning and structural analysis of the Escherichia coli ptsH, ptsI, and crr genes. , 1987, The Journal of biological chemistry.

[21]  G. Robillard,et al.  Escherichia coli Phosphoenolpyruvate Dependent Phosphotransferase System : Complete Purification of Enzyme I by Hydrophobic Interaction Chromatography , 1979 .

[22]  F. Neidhardt,et al.  Regulation of lac Operon Expression: Reappraisal of the Theory of Catabolite Repression , 1978, Journal of bacteriology.

[23]  J. Hesse,et al.  Adenosine 3':5'-cyclic monophosphate as mediator of catabolite repression in Escherichia coli. , 1975, Proceedings of the National Academy of Sciences of the United States of America.

[24]  S. Roseman,et al.  PHOSPHATE BOUND TO HISTIDINE IN A PROTEIN AS AN INTERMEDIATE IN A NOVEL PHOSPHO-TRANSFERASE SYSTEM. , 1964, Proceedings of the National Academy of Sciences of the United States of America.

[25]  B. Magasanik.  Catabolite repression. , 1961, Cold Spring Harbor symposia on quantitative biology.