Mind your B's and R's: bacterial chemotaxis, signal transduction and protein recognition.

The crystal structures of two key regulators of the bacterial chemotaxis pathway (CheR and CheB) have been determined. These studies add further detail to the growing picture of signal transduction and attenuation in the bacterial chemotaxis pathway. The recently determined structure of the methyltransferase CheR bound to a peptide of its target receptor, provides a structural model for intermolecular receptor modification during signaling.

[1]  Ann M Stock,et al.  Bacterial chemotaxis: a field in motion. , 1995, Current opinion in structural biology.

[2]  R. Weis,et al.  The receptor binding site for the methyltransferase of bacterial chemotaxis is distinct from the sites of methylation. , 1996, Biochemistry.

[3]  M. Simon,et al.  Uncoupled Phosphorylation and Activation in Bacterial Chemotaxis , 1997, The Journal of Biological Chemistry.

[4]  L E Kay,et al.  Structure and dynamics of a CheY-binding domain of the chemotaxis kinase CheA determined by nuclear magnetic resonance spectroscopy. , 1996, Biochemistry.

[5]  J. S. Parkinson,et al.  Communication modules in bacterial signaling proteins. , 1992, Annual review of genetics.

[6]  The cytoplasmic fragment of the aspartate receptor displays globally dynamic behavior. , 1996, Biochemistry.

[7]  D. Koshland.  Chemotaxis as a model second-messenger system. , 1988, Biochemistry.

[8]  S. Kim,et al.  Apo structure of the ligand‐binding domain of aspartate receptor from Escherichia coli and its comparison with ligand‐bound or pseudoligand‐bound structures , 1997, FEBS letters.

[9]  P. Matsumura,et al.  Uncoupled Phosphorylation and Activation in Bacterial Chemotaxis , 1995, The Journal of Biological Chemistry.

[10]  Ann M Stock,et al.  Crystal structure of the catalytic domain of the chemotaxis receptor methylesterase, CheB. , 1995, Journal of molecular biology.

[11]  F. Quiocho,et al.  The 2.3-A resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis. , 1992 .

[12]  J. Stock,et al.  Bacterial chemotaxis: The five sensors of a bacterium , 1998, Current Biology.

[13]  Joanne I. Yeh,et al.  Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand. , 1995, Science.

[14]  J. S. Parkinson.  Signal transduction schemes of bacteria , 1993, Cell.

[15]  Barry L. Stoddard,et al.  DNA binding and cleavage by the nuclear intron-encoded homing endonuclease I-PpoI , 1998, Nature.

[16]  S. Mowbray,et al.  The 1.9 A x-ray structure of a closed unliganded form of the periplasmic glucose/galactose receptor from Salmonella typhimurium. , 1994, The Journal of biological chemistry.

[17]  Ann M Stock,et al.  Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S-adenosylmethionine. , 1997, Structure.

[18]  S. Mowbray,et al.  Crystal structure of the dipeptide binding protein from Escherichia coli involved in active transport and chemotaxis , 1995, Protein science : a publication of the Protein Society.

[19]  Joanne I. Yeh,et al.  Refined structures of the ligand-binding domain of the aspartate receptor from Salmonella typhimurium. , 1993, Journal of molecular biology.

[20]  F. Quiocho,et al.  Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis. , 1992, Biochemistry.

[21]  D. Bray,et al.  Receptor clustering as a cellular mechanism to control sensitivity , 1998, Nature.

[22]  A. Lupas,et al.  Phosphorylation of an N-terminal regulatory domain activates the CheB methylesterase in bacterial chemotaxis. , 1989, The Journal of biological chemistry.

[23]  M. Welch,et al.  Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY , 1998, Nature Structural Biology.

[24]  Ann M Stock,et al.  Chemotaxis receptor recognition by protein methyltransferase CheR , 1998, Nature Structural Biology.

[25]  G. L. Hazelbauer,et al.  High- and low-abundance chemoreceptors in Escherichia coli: differential activities associated with closely related cytoplasmic domains , 1997, Journal of bacteriology.

[26]  L. Shapiro,et al.  Polar location of the chemoreceptor complex in the Escherichia coli cell. , 1993, Science.

[27]  R. Meadows,et al.  Structural basis for IL-4 receptor phosphopeptide recognition by thelRS-1 PTB domain , 1996, Nature Structural Biology.

[28]  M. Simon,et al.  NMR studies of the phosphotransfer domain of the histidine kinase CheA from Escherichia coli: assignments, secondary structure, general fold, and backbone dynamics. , 1995, Biochemistry.

[29]  Ann M Stock,et al.  Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain. , 1998, Proceedings of the National Academy of Sciences of the United States of America.

[30]  J. Stock,et al.  Bacterial chemotaxis and the molecular logic of intracellular signal transduction networks. , 1991, Annual review of biophysics and biophysical chemistry.

[31]  R. Weis,et al.  The serine chemoreceptor from Escherichia coli is methylated through an inter-dimer process. , 1997, Biochemistry.

[32]  D. Koshland,et al.  Global flexibility in a sensory receptor: a site-directed cross-linking approach. , 1987, Science.

[33]  J. Adler,et al.  Protein methylation in behavioural control mechanisms and in signal transduction , 1979, Nature.

[34]  D. Koshland,et al.  Methylation of the Escherichia coli chemotaxis receptors: intra- and interdimer mechanisms. , 1997, Biochemistry.

[35]  G. Petsko,et al.  Structure of the Mg(2+)-bound form of CheY and mechanism of phosphoryl transfer in bacterial chemotaxis. , 1994, Biochemistry.

[36]  Joanne I. Yeh,et al.  The three-dimensional structure of the ligand-binding domain of a wild-type bacterial chemotaxis receptor. Structural comparison to the cross-linked mutant forms and conformational changes upon ligand binding. , 1994, The Journal of biological chemistry.

[37]  R. Dickerson,et al.  Structure of the Escherichia coli response regulator NarL. , 1996, Biochemistry.