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Escherichia coli K-12 substr. MG1655 Protein: chemotaxis signaling complex - ribose/galactose/glucose sensing

Synonyms: MCP-III signaling complex

Subunit composition of chemotaxis signaling complex - ribose/galactose/glucose sensing = [(CheA)2][CheW]2[(Trg)2]3
         CheA(L) histidine kinase = (CheA)2
         methyl accepting chemotaxis protein - ribose/galactose/glucose sensing = (Trg)2 (extended summary available)

Alternative forms of chemotaxis signaling complex - ribose/galactose/glucose sensing:
Trgglu-Me
Trgglu
Trggln

Summary:
Chemotaxis in Escherichia coli is accomplished with a modified two-component signal transduction complex which transmits controlling signals to the flagellar motor complex. E.coli has four methyl-accepting chemotaxis protein (MCP)-type receptor complexes which recognize the following ligands: Tsr, serine;Tar, aspartate and maltose;Trg, ribose, galactose and glucose and Tap, dipeptides. Serine and aspartate bind directly to the receptor whereas maltose, ribose, galactose, glucose and dipeptides bind first to a periplasmic binding protein which then docks with its individual membrane receptor [Manson98].

The receptor complexes are ternary structures. The receptor-ligand interaction domain is located in the periplasm. Each receptor serves as the organizational framework for a receptor kinase signaling supermolecular complex formed in conjunction with histidine kinase CheA and other components of the signaling pathway [Falke97]. There are two transmembrane (TM) linker domains (CheW) which couple the methylation-dependent receptor to CheA. The receptors form homodimers with or without ligands [Gegner92]. CheA is a histidine kinase capable of autophosphorylation using ATP as a phosphodonor. The receptor complex dimers form trigonal units which in turn form a two-dimensional hexagonal lattice [Shimizu00] located usually at one pole of the cell. The Tsr and Tar receptors are the most abundant and the Tap, Trg receptors are less prevalent [Bren00].

CheA and CheY comprise a two-component signal transduction system where the signal is transmitted via phosphorylation from CheA to CheY (the response regulator). In several ways CheA/CheY differs from the standard two-component paradigm. Most significantly, CheY does not possess a DNA-binding domain and it doesn't act as a transcription factor. In the absence of activator ligand, CheA autophosphorylation is stimulated thus increasing the phosphotransfer from CheA to CheY, the messenger protein. CheY-P has a lower affinity for CheA than CheY, resulting in the dissociation of CheY-P from CheA. CheY-P has a higher affinity than CheY for the flagellar motor protein, FliM, a component of the motor supramolecular complex [Welch93]. Binding of CheY to FliM increases the probability of flagellar rotation in the CW direction [Barak92a]. CCW rotation of the motor induces the flagellar filaments to coalesce into a bundle which propels the cell forward in a fairly straight line (run). CW rotation disrupts the bundle and causes the cell to tumble. The cell typically travels in a three-dimensional walk consisting of runs interspersed with random chaotic tumbling. CheZ is a cytosolic phosphatase which prevents overaccumulation of CheY-P by accelerating the decay of its aspartyl-phosphate residue [Hess87].

CheY-P is thus maintained during steady-state conditions at a level that generates the random walk [Manson98]. When an attractant molecule binds to the receptor, a conformational change is induced [Yeh93] which propagates across the membrane and results in a suppression of CheA autophosphorylation. Levels of CheY-P decrease and the cells tumble less frequently, causing an increase in their run lengths as they enter areas of higher attractant concentrations. The adaptation response is necessary, though, for the cells to respond properly to continually increasing attractant concentration. Adaptive methylation is carried out by two enzymes: the methyltransferase CheR and the methylesterase CheB [Toews79]. CheR is a constitutive enzyme which, through the use of S-adenosylmethionine, methylates glutamate residues in the cytoplasmic domains of the MCPs. CheB is a target for phosphotransfer from CheA, and the activated CheB-P functions as a methyl esterase which removes methyl groups from the MCPs, reducing their kinase activity. Under steady-state conditions, the addition of methyl groups by CheR is balanced by the methyl group removal by CheB-P and an intermediate level of receptor methylation is maintained, resulting in run-tumble behavior of the cell. When an attractant binds to a receptor and inhibits CheA activity, the levels of CheB-P drop. The decrease is slower than that for CheY-P though, since CheB-P is not a phosphate donor to CheZ. The rising level of methyl esters eventually stimulate histidine kinase activity and therefore counteract the effect of attractant binding to the receptor. This resets the receptor signal to its basal level [Falke97].

The components of the chemotaxis sensory system are arranged at one of the cell poles in tight clusters containing thousands of copies of each protein [Sourjik00]. Binding of an attractant results in an increase in the probability that CheA is inactive (unphosphorylated) and methylation of CheA on four specific glutamate residues increases the probability that that it is active (phosphorylated) [Borkovich92]. Lower levels of methylation reduce the activity of CheA but increase the affinity of the receptor for its attractant ligand [Li00b].

Gene-Reaction Schematic: ?


Subunit of chemotaxis signaling complex - ribose/galactose/glucose sensing: CheA(L) histidine kinase

Synonyms: chemotaxis kinase-phosphotransferase CheA(L)

Gene: cheA Accession Numbers: EG10146 (EcoCyc), b1888, ECK1889

Locations: inner membrane, cytosol

Subunit composition of CheA(L) histidine kinase = [CheA]2

Map Position: [1,971,384 <- 1,973,348] (42.49 centisomes)
Length: 1965 bp / 654 aa

Molecular Weight of Polypeptide: 71.382 kD (from nucleotide sequence)

pI: 4.96

GO Terms:

Biological Process: GO:0000160 - phosphorelay signal transduction system Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA01, Igo89]
GO:0016310 - phosphorylation Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA01, Igo89]
GO:0031400 - negative regulation of protein modification process Inferred from experiment [Barak04a]
GO:0046777 - protein autophosphorylation Inferred from experiment [Igo89]
GO:0006935 - chemotaxis Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0007165 - signal transduction Inferred by computational analysis [GOA01]
GO:0018106 - peptidyl-histidine phosphorylation Inferred by computational analysis [GOA01a, GOA01]
GO:0023014 - signal transduction by phosphorylation Inferred by computational analysis [GOA01]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Thakor11, Rajagopala09, OConnor09, Hao09]
GO:0000155 - phosphorelay sensor kinase activity Inferred by computational analysis [GOA01]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11]
GO:0004673 - protein histidine kinase activity Inferred by computational analysis [GOA01a]
GO:0004871 - signal transducer activity Inferred by computational analysis [GOA01]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11]
GO:0016301 - kinase activity Inferred by computational analysis [UniProtGOA11]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11]
GO:0016772 - transferase activity, transferring phosphorus-containing groups Inferred by computational analysis [GOA01]
Cellular Component: GO:0005829 - cytosol Inferred from experiment [Ridgway77]
GO:0005886 - plasma membrane Inferred from experiment [Ridgway77]
GO:0005622 - intracellular Inferred by computational analysis [GOA01]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, GOA01]

MultiFun Terms: cell processes motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
information transfer protein related posttranslational modification

Unification Links: EcoliWiki:b1888 , ModBase:P07363 , Swiss-Model:P07363

Relationship Links: UniProt:RELATED-TO:P07363

Reactions known to consume the compound:

Aerotactic Two-Component Signal Transduction System , Chemotactic Two-Component Signal Transduction :
CheA + ATP → CheA-P + ADP

Reactions known to produce the compound:

Aerotactic Two-Component Signal Transduction System :
CheY + CheA-P → CheY-Pasp + CheA

Chemotactic Two-Component Signal Transduction :
CheA-P + CheB → CheA + CheB-Pasp
CheY + CheA-P → CheY-Pasp + CheA

Summary:
The cheA gene is translated in two isoforms. The small form, CheA(S), arises due to a second translational start site 291 bases downstream of the translation start site for the large form, CheA(L) [Hoch95, Neidhardt96].

The "Spliced Nucleotide Sequence" link above refers to the smaller variant, but note that no splicing occurs.
CheA is the histidine kinase component of the chemotaxis two-component signal transduction complex. The chemotaxis system propagates changes in extracellular chemical concentrations to the flagellar switch complex to regulate swimming behavior. CheA and CheY comprise a two-component signal transduction system where the signal generated by the periplasmic receptor occupancy through a protein-protein interaction with the CheA cytoplasmic component is transmitted via phosphorylation from autophosphorylating histidine kinase CheA to CheY (the response regulator) [Welch93]. The receptor complexes (MCPI, MCPII, MCPIII and MCPIV) are ternary structures consisting of receptors, CheA and the adaptor protein CheW.

Escherichia coli expresses CheA as both a full length molecule as well as a shorter version translated from an alternative start codon known as CheA(short), which contains a catalytic domain but no kinase substrate domain [Kofoid91]. As a result, a heterodimer containing a full-length CheA alongside a CheA(s) exhibits a fivefold higher autophosphorylation rate than the CheA homodimer [Levit96].

CheA autophosphorylates on His48 in the presence of ATP in vitro. The phosphate group on CheA can be transferred to CheB or to CheY in vitro [Hess88, Hess88a]. CheA is a dimer in solution. Two CheW monomers bind per CheA dimer [Gegner91]. CheA autophosphorylation results from transphosphorylation within the dimer [Swanson93]. In an in vitro reconstituted system, autophosphorylation of purified CheA is stimulated by addition of wild type Tar receptor and CheW protein [Borkovich90, Borkovich89]. CheA contains separate functional domains associated with kinase activity, CheY binding, phosphotransfer activity and receptor binding [Swanson93a, Bourret93, Morrison94, Stewart00, Stewart04, Bhatnagar12]. CheA interacts with chemoreceptors in a manner similar to CheW; CheA and CheW bind to the same region of chemoreceptors due to structural similarity between CheW and the regulatory or P5 domain of CheA [Wang12]. Chemotaxis receptors control kinase activity by regulating CheA domain mobility [Briegel13].

Citations: [Zhao06a, Levit02, Francis04, Morrison97, Piasta13, Garzon96, Thakor11]

Gene Citations: [Silverman77a, Mirel92]

Essentiality data for cheA knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of chemotaxis signaling complex - ribose/galactose/glucose sensing: CheW

Synonyms: purine-binding chemotaxis protein

Gene: cheW Accession Numbers: EG10149 (EcoCyc), b1887, ECK1888

Locations: cytosol

Sequence Length: 167 AAs

Molecular Weight [Bairoch93]: 18.084 kD (from nucleotide sequence)

pI: 4.54

GO Terms:

Biological Process: GO:0006935 - chemotaxis Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA01, Liu89a]
GO:0007165 - signal transduction Inferred from experiment Inferred by computational analysis [GOA01, Gegner91, Liu89a]
GO:0051649 - establishment of localization in cell Inferred from experiment [Kentner06]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Arifuzzaman06, Rajagopala09]
GO:0004871 - signal transducer activity Inferred by computational analysis [GOA01]
Cellular Component: GO:0005829 - cytosol Inferred from experiment [Ridgway77]
GO:0005622 - intracellular Inferred by computational analysis [GOA01]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11a, UniProtGOA11]

MultiFun Terms: cell processes motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
regulation type of regulation posttranscriptional inhibition / activation of enzymes

Unification Links: DIP:DIP-48236N , EcoliWiki:b1887 , Mint:MINT-1283783 , ModBase:P0A964 , PR:PRO_000022280 , Protein Model Portal:P0A964 , RefSeq:NP_416401 , SMR:P0A964 , String:511145.b1887 , UniProt:P0A964

Relationship Links: InterPro:IN-FAMILY:IPR002545 , PDB:Structure:2HO9 , Pfam:IN-FAMILY:PF01584 , Prosite:IN-FAMILY:PS50851 , Smart:IN-FAMILY:SM00260

Summary:
CheW is involved in the transmission of sensory signals from the methyl-accepting chemotaxis proteins (MCPs) to the flagellar motors. CheW provides a physical coupling of CheA to the MCPs allowing regulated phosphotransfer to the CheY and CheB proteins. When CheW is complexed with CheA(L) and CheA(S) in a 1:1:1 ratio the autophosphorylation rate of CheA is increased [Bairoch93, Gegner91, Liu89a, McNally91, Liu97a, Neidhardt96]. Excess levels of CheW disrupt CheA activation and chemotactic response [Liu89a, Sanders89, Boukhvalova02] possibly by disrupting the normal formation of receptor complexes [Studdert05, Cardozo10].

Citations: [Underbakke11]

Essentiality data for cheW knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of chemotaxis signaling complex - ribose/galactose/glucose sensing: methyl accepting chemotaxis protein - ribose/galactose/glucose sensing

Synonyms: MCP-III, ribose/galactose/glucose chemoreceptor protein, Trg dimer, chemotaxis signaling protein III

Gene: trg Accession Numbers: EG11018 (EcoCyc), b1421, ECK1415

Locations: inner membrane

Subunit composition of methyl accepting chemotaxis protein - ribose/galactose/glucose sensing = [Trg]2

Map Position: [1,490,494 -> 1,492,134] (32.12 centisomes)
Length: 1641 bp / 546 aa

Molecular Weight of Polypeptide: 58.899 kD (from nucleotide sequence)

pI: 6.61

GO Terms:

Biological Process: GO:0006935 - chemotaxis Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA01, Kondoh79]
GO:0007165 - signal transduction Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA01, Kondoh79, Hughson96]
Molecular Function: GO:0004888 - transmembrane signaling receptor activity Inferred from experiment Inferred by computational analysis [GOA01, Kondoh79, Hughson96]
GO:0005515 - protein binding Inferred from experiment [Rajagopala14]
GO:0004871 - signal transducer activity Inferred by computational analysis [UniProtGOA11, GOA01]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, DiazMejia09, Zhang07, Daley05, Hazelbauer81]
GO:0005887 - integral component of plasma membrane Inferred by computational analysis [Bollinger84]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11, GOA01]

MultiFun Terms: cell processes motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
cell structure membrane
regulation type of regulation posttranscriptional inhibition / activation of enzymes

Unification Links: DIP:DIP-11027N , EcoliWiki:b1421 , Mint:MINT-1228342 , ModBase:P05704 , PR:PRO_000024111 , Protein Model Portal:P05704 , RefSeq:NP_415938 , SMR:P05704 , String:511145.b1421 , Swiss-Model:P05704 , UniProt:P05704

Relationship Links: InterPro:IN-FAMILY:IPR003122 , InterPro:IN-FAMILY:IPR003660 , InterPro:IN-FAMILY:IPR004089 , InterPro:IN-FAMILY:IPR004090 , InterPro:IN-FAMILY:IPR004091 , Pfam:IN-FAMILY:PF00015 , Pfam:IN-FAMILY:PF00672 , Pfam:IN-FAMILY:PF02203 , Prints:IN-FAMILY:PR00260 , Prosite:IN-FAMILY:PS00538 , Prosite:IN-FAMILY:PS50111 , Prosite:IN-FAMILY:PS50885 , Smart:IN-FAMILY:SM00283 , Smart:IN-FAMILY:SM00304 , Smart:IN-FAMILY:SM00319

Summary:
The trg gene product is one of four methyl-accepting chemotaxis proteins (MCPs) in E. coli. MCP-III is the receptor for the attractants ribose and galactose. MCP-III interacts with the periplasmic ribose- or galactose-binding proteins to mediate taxis to these attractants [Hazelbauer71, Kondoh79, Yaghmai93]. It is also thermosensitive [Nara91]. trg expressed from a plasmid in an E. coli strain lacking all four MCPs, mediates a repellent response to phenol [Yamamoto90].

E. coli Trg is a homodimeric inner membrane protein; the Trg monomer consists of a periplasmic, ligand-sensing domain, two trans-membrane segments (TM1 and TM2) and a cytoplasmic signaling domain predicted to contain 5 methylation sites [Kehry83, Nowlin87, Bollinger84, Nowlin88, Lee94]. Methylation and demethylation of MCPs in E. coli K-12 is catalysed by the CheR methyltransferase and the CheB methylesterase. Two methyl accepting residues arise from CheB catalysed post-translational deamidation of glutamines to yield glutamates [Engstrom83].

The cytoplasmic domains of the four E. coli MCPs have a high degree of sequence similarity [Krikos83, Le96, Alexander07].Trg contains a HAMP domain (present in histidine kinases, adenylate cyclases, methyl accepting chemotaxis proteins, phosphatases) which is located between the transmembrane region of the molecule and the cytoplasmic signalling region. HAMP domains are thought to mediate input/ouptut signaling (reviewed in [Parkinson10].

Trg and Tap are considered to be low-abundance receptors while Tsr and Tar are considered to be high-abundance [Hazelbauer81, Hazelbauer81a, Harayama82]

trg: taxis to ribose and galactose

Reviews: [Stock00, Hazelbauer08]

Citations: [Parkinson75, Hazelbauer89, Yang79, Lee95, Baumgartner96, Lee95a, Hughson96, Beel01, Park86, Hazelbauer69, Adler73]

Essentiality data for trg knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

References

Adler73: Adler J, Hazelbauer GL, Dahl MM (1973). "Chemotaxis toward sugars in Escherichia coli." J Bacteriol 115(3);824-47. PMID: 4580570

Alexander07: Alexander RP, Zhulin IB (2007). "Evolutionary genomics reveals conserved structural determinants of signaling and adaptation in microbial chemoreceptors." Proc Natl Acad Sci U S A 104(8);2885-90. PMID: 17299051

Arifuzzaman06: Arifuzzaman M, Maeda M, Itoh A, Nishikata K, Takita C, Saito R, Ara T, Nakahigashi K, Huang HC, Hirai A, Tsuzuki K, Nakamura S, Altaf-Ul-Amin M, Oshima T, Baba T, Yamamoto N, Kawamura T, Ioka-Nakamichi T, Kitagawa M, Tomita M, Kanaya S, Wada C, Mori H (2006). "Large-scale identification of protein-protein interaction of Escherichia coli K-12." Genome Res 16(5);686-91. PMID: 16606699

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Bairoch93: Bairoch A, Boeckmann B (1993). "The SWISS-PROT protein sequence data bank, recent developments." Nucleic Acids Res. 21:3093-3096. PMID: 8332529

Barak04a: Barak R, Eisenbach M (2004). "Co-regulation of acetylation and phosphorylation of CheY, a response regulator in chemotaxis of Escherichia coli." J Mol Biol 342(2);375-81. PMID: 15327941

Barak92a: Barak R, Eisenbach M (1992). "Correlation between phosphorylation of the chemotaxis protein CheY and its activity at the flagellar motor." Biochemistry 31(6);1821-6. PMID: 1737035

Baumgartner96: Baumgartner JW, Hazelbauer GL (1996). "Mutational analysis of a transmembrane segment in a bacterial chemoreceptor." J Bacteriol 1996;178(15);4651-60. PMID: 8755897

Beel01: Beel BD, Hazelbauer GL (2001). "Signalling substitutions in the periplasmic domain of chemoreceptor Trg induce or reduce helical sliding in the transmembrane domain." Mol Microbiol 40(4);824-34. PMID: 11401690

Bhatnagar12: Bhatnagar J, Sircar R, Borbat PP, Freed JH, Crane BR (2012). "Self-association of the histidine kinase CheA as studied by pulsed dipolar ESR spectroscopy." Biophys J 102(9);2192-201. PMID: 22824284

Bollinger84: Bollinger J, Park C, Harayama S, Hazelbauer GL (1984). "Structure of the Trg protein: Homologies with and differences from other sensory transducers of Escherichia coli." Proc Natl Acad Sci U S A 1984;81(11);3287-91. PMID: 6374654

Borkovich89: Borkovich KA, Kaplan N, Hess JF, Simon MI (1989). "Transmembrane signal transduction in bacterial chemotaxis involves ligand-dependent activation of phosphate group transfer." Proc Natl Acad Sci U S A 86(4);1208-12. PMID: 2645576

Borkovich90: Borkovich KA, Simon MI (1990). "The dynamics of protein phosphorylation in bacterial chemotaxis." Cell 63(6);1339-48. PMID: 2261645

Borkovich92: Borkovich KA, Alex LA, Simon MI (1992). "Attenuation of sensory receptor signaling by covalent modification." Proc Natl Acad Sci U S A 89(15);6756-60. PMID: 1495964

Boukhvalova02: Boukhvalova MS, Dahlquist FW, Stewart RC (2002). "CheW binding interactions with CheA and Tar. Importance for chemotaxis signaling in Escherichia coli." J Biol Chem 277(25);22251-9. PMID: 11923283

Bourret93: Bourret RB, Davagnino J, Simon MI (1993). "The carboxy-terminal portion of the CheA kinase mediates regulation of autophosphorylation by transducer and CheW." J Bacteriol 175(7);2097-101. PMID: 8384620

Bren00: Bren A, Eisenbach M (2000). "How signals are heard during bacterial chemotaxis: protein-protein interactions in sensory signal propagation." J Bacteriol 182(24);6865-73. PMID: 11092844

Briegel13: Briegel A, Ames P, Gumbart JC, Oikonomou CM, Parkinson JS, Jensen GJ (2013). "The mobility of two kinase domains in the Escherichia coli chemoreceptor array varies with signalling state." Mol Microbiol 89(5);831-41. PMID: 23802570

Cardozo10: Cardozo MJ, Massazza DA, Parkinson JS, Studdert CA (2010). "Disruption of chemoreceptor signalling arrays by high levels of CheW, the receptor-kinase coupling protein." Mol Microbiol 75(5);1171-81. PMID: 20487303

Daley05: Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308(5726);1321-3. PMID: 15919996

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Engstrom83: Engstrom P, Nowlin D, Bollinger J, Magnuson N, Hazelbauer GL (1983). "Limited homology between trg and the other transducer proteins of Escherichia coli." J Bacteriol 156(3);1268-74. PMID: 6358194

Falke97: Falke JJ, Bass RB, Butler SL, Chervitz SA, Danielson MA (1997). "The two-component signaling pathway of bacterial chemotaxis: a molecular view of signal transduction by receptors, kinases, and adaptation enzymes." Annu Rev Cell Dev Biol 13;457-512. PMID: 9442881

Francis04: Francis NR, Wolanin PM, Stock JB, Derosier DJ, Thomas DR (2004). "Three-dimensional structure and organization of a receptor/signaling complex." Proc Natl Acad Sci U S A 101(50);17480-5. PMID: 15572451

Garzon96: Garzon A, Parkinson JS (1996). "Chemotactic signaling by the P1 phosphorylation domain liberated from the CheA histidine kinase of Escherichia coli." J Bacteriol 178(23);6752-8. PMID: 8955292

Gegner91: Gegner JA, Dahlquist FW (1991). "Signal transduction in bacteria: CheW forms a reversible complex with the protein kinase CheA." Proc Natl Acad Sci U S A 1991;88(3);750-4. PMID: 1992467

Gegner92: Gegner JA, Graham DR, Roth AF, Dahlquist FW (1992). "Assembly of an MCP receptor, CheW, and kinase CheA complex in the bacterial chemotaxis signal transduction pathway." Cell 70(6);975-82. PMID: 1326408

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

Hao09: Hao S, Hamel D, Zhou H, Dahlquist FW (2009). "Structural basis for the localization of the chemotaxis phosphatase CheZ by CheAS." J Bacteriol 191(18);5842-4. PMID: 19502407

Harayama82: Harayama S, Engstrom P, Wolf-Watz H, Iino T, Hazelbauer GL (1982). "Cloning of trg, a gene for a sensory transducer in Escherichia coli." J Bacteriol 152(1);372-83. PMID: 6749811

Hazelbauer08: Hazelbauer GL, Falke JJ, Parkinson JS (2008). "Bacterial chemoreceptors: high-performance signaling in networked arrays." Trends Biochem Sci 33(1);9-19. PMID: 18165013

Hazelbauer69: Hazelbauer GL, Mesibov RE, Adler J (1969). "Escherichia coli mutants defective in chemotaxis toward specific chemicals." Proc Natl Acad Sci U S A 64(4);1300-7. PMID: 4916925

Hazelbauer71: Hazelbauer GL, Adler J (1971). "Role of the galactose binding protein in chemotaxis of Escherichia coli toward galactose." Nat New Biol 230(12);101-4. PMID: 4927373

Hazelbauer81: Hazelbauer GL, Engstrom P, Harayama S (1981). "Methyl-accepting chemotaxis protein III and transducer gene trg." J Bacteriol 145(1);43-9. PMID: 7007323

Hazelbauer81a: Hazelbauer GL, Engstrom P (1981). "Multiple forms of methyl-accepting chemotaxis proteins distinguished by a factor in addition to multiple methylation." J Bacteriol 145(1);35-42. PMID: 7007319

Hazelbauer89: Hazelbauer GL, Park C, Nowlin DM (1989). "Adaptational "crosstalk" and the crucial role of methylation in chemotactic migration by Escherichia coli." Proc Natl Acad Sci U S A 1989;86(5);1448-52. PMID: 2646634

Hess87: Hess JF, Oosawa K, Matsumura P, Simon MI (1987). "Protein phosphorylation is involved in bacterial chemotaxis." Proc Natl Acad Sci U S A 1987;84(21);7609-13. PMID: 3313398

Hess88: Hess JF, Bourret RB, Simon MI (1988). "Histidine phosphorylation and phosphoryl group transfer in bacterial chemotaxis." Nature 1988;336(6195);139-43. PMID: 3185734

Hess88a: Hess JF, Oosawa K, Kaplan N, Simon MI (1988). "Phosphorylation of three proteins in the signaling pathway of bacterial chemotaxis." Cell 1988;53(1);79-87. PMID: 3280143

Hoch95: Hoch, JA, Silhavy, TJ "Two-Component Signal Transduction." ASM Press, Washington, D.C. 1995.

Hughson96: Hughson AG, Hazelbauer GL (1996). "Detecting the conformational change of transmembrane signaling in a bacterial chemoreceptor by measuring effects on disulfide cross-linking in vivo." Proc Natl Acad Sci U S A 93(21);11546-51. PMID: 8876172

Igo89: Igo MM, Ninfa AJ, Stock JB, Silhavy TJ (1989). "Phosphorylation and dephosphorylation of a bacterial transcriptional activator by a transmembrane receptor." Genes Dev 3(11);1725-34. PMID: 2558046

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Kehry83: Kehry MR, Engstrom P, Dahlquist FW, Hazelbauer GL (1983). "Multiple covalent modifications of Trg, a sensory transducer of Escherichia coli." J Biol Chem 258(8);5050-5. PMID: 6300110

Kentner06: Kentner D, Thiem S, Hildenbeutel M, Sourjik V (2006). "Determinants of chemoreceptor cluster formation in Escherichia coli." Mol Microbiol 61(2);407-17. PMID: 16856941

Kofoid91: Kofoid EC, Parkinson JS (1991). "Tandem translation starts in the cheA locus of Escherichia coli." J Bacteriol 173(6);2116-9. PMID: 2002011

Kondoh79: Kondoh H, Ball CB, Adler J (1979). "Identification of a methyl-accepting chemotaxis protein for the ribose and galactose chemoreceptors of Escherichia coli." Proc Natl Acad Sci U S A 1979;76(1);260-4. PMID: 370826

Krikos83: Krikos A, Mutoh N, Boyd A, Simon MI (1983). "Sensory transducers of E. coli are composed of discrete structural and functional domains." Cell 1983;33(2);615-22. PMID: 6305515

Le96: Le Moual H, Koshland DE (1996). "Molecular evolution of the C-terminal cytoplasmic domain of a superfamily of bacterial receptors involved in taxis." J Mol Biol 261(4);568-85. PMID: 8794877

Lee94: Lee GF, Burrows GG, Lebert MR, Dutton DP, Hazelbauer GL (1994). "Deducing the organization of a transmembrane domain by disulfide cross-linking. The bacterial chemoreceptor Trg." J Biol Chem 1994;269(47);29920-7. PMID: 7961989

Lee95: Lee GF, Lebert MR, Lilly AA, Hazelbauer GL (1995). "Transmembrane signaling characterized in bacterial chemoreceptors by using sulfhydryl cross-linking in vivo." Proc Natl Acad Sci U S A 1995;92(8);3391-5. PMID: 7724572

Lee95a: Lee GF, Hazelbauer GL (1995). "Quantitative approaches to utilizing mutational analysis and disulfide crosslinking for modeling a transmembrane domain." Protein Sci 4(6);1100-7. PMID: 7549874

Levit02: Levit MN, Grebe TW, Stock JB (2002). "Organization of the receptor-kinase signaling array that regulates Escherichia coli chemotaxis." J Biol Chem 277(39);36748-54. PMID: 12119289

Levit96: Levit M, Liu Y, Surette M, Stock J (1996). "Active site interference and asymmetric activation in the chemotaxis protein histidine kinase CheA." J Biol Chem 271(50);32057-63. PMID: 8943256

Li00b: Li G, Weis RM (2000). "Covalent modification regulates ligand binding to receptor complexes in the chemosensory system of Escherichia coli." Cell 100(3);357-65. PMID: 10676817

Liu89a: Liu JD, Parkinson JS (1989). "Role of CheW protein in coupling membrane receptors to the intracellular signaling system of bacterial chemotaxis." Proc Natl Acad Sci U S A 1989;86(22);8703-7. PMID: 2682657

Liu97a: Liu Y, Levit M, Lurz R, Surette MG, Stock JB (1997). "Receptor-mediated protein kinase activation and the mechanism of transmembrane signaling in bacterial chemotaxis." EMBO J 1997;16(24);7231-40. PMID: 9405352

Manson98: Manson MD, Armitage JP, Hoch JA, Macnab RM (1998). "Bacterial locomotion and signal transduction." J Bacteriol 180(5);1009-22. PMID: 9495737

McNally91: McNally DF, Matsumura P (1991). "Bacterial chemotaxis signaling complexes: formation of a CheA/CheW complex enhances autophosphorylation and affinity for CheY." Proc Natl Acad Sci U S A 1991;88(14);6269-73. PMID: 2068106

Mirel92: Mirel DB, Lustre VM, Chamberlin MJ (1992). "An operon of Bacillus subtilis motility genes transcribed by the sigma D form of RNA polymerase." J Bacteriol 1992;174(13);4197-204. PMID: 1624413

Morrison94: Morrison TB, Parkinson JS (1994). "Liberation of an interaction domain from the phosphotransfer region of CheA, a signaling kinase of Escherichia coli." Proc Natl Acad Sci U S A 91(12);5485-9. PMID: 8202513

Morrison97: Morrison TB, Parkinson JS (1997). "A fragment liberated from the Escherichia coli CheA kinase that blocks stimulatory, but not inhibitory, chemoreceptor signaling." J Bacteriol 179(17);5543-50. PMID: 9287011

Nara91: Nara T, Lee L, Imae Y (1991). "Thermosensing ability of Trg and Tap chemoreceptors in Escherichia coli." J Bacteriol 1991;173(3);1120-4. PMID: 1991711

Neidhardt96: Neidhardt FC, Curtiss III R, Ingraham JL, Lin ECC, Low Jr KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE "Escherichia coli and Salmonella, Cellular and Molecular Biology, Second Edition." American Society for Microbiology, Washington, D.C., 1996.

Nowlin87: Nowlin DM, Bollinger J, Hazelbauer GL (1987). "Sites of covalent modification in Trg, a sensory transducer of Escherichia coli." J Biol Chem 1987;262(13);6039-45. PMID: 3032955

Nowlin88: Nowlin DM, Bollinger J, Hazelbauer GL (1988). "Site-directed mutations altering methyl-accepting residues of a sensory transducer protein." Proteins 3(2);102-12. PMID: 3041407

OConnor09: O'Connor C, Matsumura P, Campos A (2009). "The CheZ binding interface of CheAS is located in alpha-helix E." J Bacteriol 191(18);5845-8. PMID: 19581362

Park86: Park C, Hazelbauer GL (1986). "Mutations specifically affecting ligand interaction of the Trg chemosensory transducer." J Bacteriol 167(1);101-9. PMID: 3087946

Parkinson10: Parkinson JS (2010). "Signaling mechanisms of HAMP domains in chemoreceptors and sensor kinases." Annu Rev Microbiol 64;101-22. PMID: 20690824

Parkinson75: Parkinson JS (1975). "Genetics of chemotactic behavior in bacteria." Cell 4(3);183-8. PMID: 235371

Piasta13: Piasta KN, Ulliman CJ, Slivka PF, Crane BR, Falke JJ (2013). "Defining a key receptor-CheA kinase contact and elucidating its function in the membrane-bound bacterial chemosensory array: a disulfide mapping and TAM-IDS Study." Biochemistry 52(22);3866-80. PMID: 23668882

Rajagopala09: Rajagopala SV, Hughes KT, Uetz P (2009). "Benchmarking yeast two-hybrid systems using the interactions of bacterial motility proteins." Proteomics 9(23);5296-302. PMID: 19834901

Rajagopala14: Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Hauser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P (2014). "The binary protein-protein interaction landscape of Escherichia coli." Nat Biotechnol 32(3);285-90. PMID: 24561554

Ridgway77: Ridgway HG, Silverman M, Simon MI (1977). "Localization of proteins controlling motility and chemotaxis in Escherichia coli." J Bacteriol 132(2);657-65. PMID: 334749

Sanders89: Sanders DA, Mendez B, Koshland DE (1989). "Role of the CheW protein in bacterial chemotaxis: overexpression is equivalent to absence." J Bacteriol 171(11);6271-8. PMID: 2681160

Shimizu00: Shimizu TS, Le Novere N, Levin MD, Beavil AJ, Sutton BJ, Bray D (2000). "Molecular model of a lattice of signalling proteins involved in bacterial chemotaxis." Nat Cell Biol 2(11);792-6. PMID: 11056533

Silverman77a: Silverman M, Simon M (1977). "Identification of polypeptides necessary for chemotaxis in Escherichia coli." J Bacteriol 1977;130(3);1317-25. PMID: 324984

Sourjik00: Sourjik V, Berg HC (2000). "Localization of components of the chemotaxis machinery of Escherichia coli using fluorescent protein fusions." Mol Microbiol 37(4);740-51. PMID: 10972797

Stewart00: Stewart RC, Jahreis K, Parkinson JS (2000). "Rapid phosphotransfer to CheY from a CheA protein lacking the CheY-binding domain." Biochemistry 39(43);13157-65. PMID: 11052668

Stewart04: Stewart RC, Van Bruggen R (2004). "Association and dissociation kinetics for CheY interacting with the P2 domain of CheA." J Mol Biol 336(1);287-301. PMID: 14741223

Stock00: Stock J, Levit M (2000). "Signal transduction: hair brains in bacterial chemotaxis." Curr Biol 10(1);R11-4. PMID: 10660286

Studdert05: Studdert CA, Parkinson JS (2005). "Insights into the organization and dynamics of bacterial chemoreceptor clusters through in vivo crosslinking studies." Proc Natl Acad Sci U S A 102(43);15623-8. PMID: 16230637

Swanson93: Swanson RV, Bourret RB, Simon MI (1993). "Intermolecular complementation of the kinase activity of CheA." Mol Microbiol 8(3);435-41. PMID: 8326858

Swanson93a: Swanson RV, Schuster SC, Simon MI (1993). "Expression of CheA fragments which define domains encoding kinase, phosphotransfer, and CheY binding activities." Biochemistry 32(30);7623-9. PMID: 8347572

Thakor11: Thakor H, Nicholas S, Porter IM, Hand N, Stewart RC (2011). "Identification of an anchor residue for CheA-CheY interactions in the chemotaxis system of Escherichia coli." J Bacteriol 193(15);3894-903. PMID: 21642453

Toews79: Toews ML, Goy MF, Springer MS, Adler J (1979). "Attractants and repellents control demethylation of methylated chemotaxis proteins in Escherichia coli." Proc Natl Acad Sci U S A 76(11);5544-8. PMID: 392505

Underbakke11: Underbakke ES, Zhu Y, Kiessling LL (2011). "Protein footprinting in a complex milieu: identifying the interaction surfaces of the chemotaxis adaptor protein CheW." J Mol Biol 409(4);483-95. PMID: 21463637

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

Wang12: Wang X, Vu A, Lee K, Dahlquist FW (2012). "CheA-receptor interaction sites in bacterial chemotaxis." J Mol Biol 422(2);282-90. PMID: 22659323

Welch93: Welch M, Oosawa K, Aizawa S, Eisenbach M (1993). "Phosphorylation-dependent binding of a signal molecule to the flagellar switch of bacteria." Proc Natl Acad Sci U S A 90(19);8787-91. PMID: 8415608

Yaghmai93: Yaghmai R, Hazelbauer GL (1993). "Strategies for differential sensory responses mediated through the same transmembrane receptor." EMBO J 1993;12(5);1897-905. PMID: 8491182

Yamamoto90: Yamamoto K, Macnab RM, Imae Y (1990). "Repellent response functions of the Trg and Tap chemoreceptors of Escherichia coli." J Bacteriol 1990;172(1);383-8. PMID: 2403544

Yang79: Yang YH, Rhim JS, Rasheed S, Klement V, Roy-Burman P (1979). "Reversion of Kirsten sarcoma virus transformed human cells: elimination of the sarcoma virus nucleotide sequences." J Gen Virol 43(2);447-51. PMID: 225428

Yeh93: Yeh JI, Biemann HP, Pandit J, Koshland DE, Kim SH (1993). "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." J Biol Chem 268(13);9787-92. PMID: 8486661

Zhang07: Zhang N, Chen R, Young N, Wishart D, Winter P, Weiner JH, Li L (2007). "Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS." Proteomics 7(4);484-93. PMID: 17309111

Zhao06a: Zhao J, Parkinson JS (2006). "Mutational analysis of the chemoreceptor-coupling domain of the Escherichia coli chemotaxis signaling kinase CheA." J Bacteriol 188(9);3299-307. PMID: 16621823


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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