Escherichia coli K-12 substr. MG1655 Protein: methyl accepting chemotaxis protein Tar

Gene: tar Accession Numbers: EG10988 (EcoCyc), b1886, ECK1887

Synonyms: cheM, MCP-II, aspartate chemoreceptor protein, Tar dimer, chemotaxis signaling protein II

Regulation Summary Diagram: ?

Regulation summary diagram for tar

Component of: chemotaxis signaling complex - aspartate sensing (extended summary available)

Subunit composition of methyl accepting chemotaxis protein Tar = [Tar]2

Alternative forms of chemotaxis signaling complex - aspartate sensing:

The tar gene product is one of four methyl-accepting chemotaxis proteins (MCPs) in E. coli K-12. MCP-II is the receptor for the attractants aspartate and maltose and the repellents nickel and cobalt [Reader79, Wang80, Springer77]. Tar is the primary receptor for the amino acids aspartate, asparagine and glutamate; in strains lacking the Tsr receptor, Tar can mediate a chemotactic response to serine, cysteine, glycine, alanine and asparagine [Yang15]. Tar is responsible for mediating an attractant response to phenol [Imae87] and Tsr and Tar mediate a chemotactic response to changes in pH [Krikos85].

E. coli Tar is a homodimeric inner membrane protein; the Tar monomer consists of a periplasmic, ligand-sensing domain, two trans-membrane segments (TM1 and TM2) and a cytoplasmic signaling domain which is predominantly alpha-helical in structure and is predicted to contain 4 methylation sites [Lynch91, Bowie95, Le96]. The cytoplasmic domain of Tar is subject to methylation and demethylation at the carboxyl groups of glutamic acid residues [DeFranco80, Engstrom80, Krikos83]. Methylation and demethylation of MCPs in E. coli K-12 is catalysed by the CheR methyltransferase and the CheB methylesterase.

Aspartate binds directly to the Tar receptor whereas maltose detection is mediated via the periplasmic maltose binding protein [Manson85, Wolff88, Mowbray87, Gardina92, Gardina97, Gardina98, Zhang99]. Aspartate binding to a purified Tar receptor generates a downward piston motion of TM1 relative to TM2 [Ottemann99]

The cytoplasmic domains of the four E. coli MCPs have a high degree of sequence similarity [Krikos83, Le96, Alexander07]. Tar 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. Tsr HAMP domains have been shown to mediate input/ouptut signaling [Ames08, Zhou09, Zhou11, Ames13, Samanta15] (and reviewed in [Parkinson10]).

E. coli MCPs form ternary complexes with the cytoplasmic proteins CheA and CheW [Gegner92]. Tar and Tsr are considered to be high-abundance receptors while Tap and Trg are low-abundance [Hazelbauer81, Hazelbauer81a, Harayama82].

Novel chemoeffectors specific for Tar have been identified as have two antagonistic compounds which bind to Tar but do not induce a chemotactic response [Bi13a].

tar: taxis to aspartate and from repellents

Comments: [Gerstein99, Stock96, Manson09, Manson11]

Citations: [Pakula92, Boyd80, Chelsky80, Stoddard92, Falke87, Wright11, Cochran96, Tatsuno96, Gardina96, Nishiyama99, Draheim05, Lai08, Hazelbauer69, Mesibov72, Mise14, Hedblom83]

Gene Citations: [Kundu97, Arnosti89, Slocum83, Parkinson82, Parkinson78]

Locations: inner membrane

Map Position: [1,969,054 <- 1,970,715] (42.44 centisomes, 153°)
Length: 1662 bp / 553 aa

Molecular Weight of Polypeptide: 59.944 kD (from nucleotide sequence), 60.0 kD (experimental) [Wang80 ]

pI: 5.73

Unification Links: ASAP:ABE-0006290 , CGSC:122 , DIP:DIP-10956N , DisProt:DP00294 , EchoBASE:EB0981 , EcoGene:EG10988 , EcoliWiki:b1886 , ModBase:P07017 , OU-Microarray:b1886 , PortEco:tar , PR:PRO_000024026 , Pride:P07017 , Protein Model Portal:P07017 , RefSeq:NP_416400 , RegulonDB:EG10988 , SMR:P07017 , String:511145.b1886 , Swiss-Model:P07017 , UniProt:P07017

Relationship Links: InterPro:IN-FAMILY:IPR003122 , InterPro:IN-FAMILY:IPR003660 , InterPro:IN-FAMILY:IPR004089 , InterPro:IN-FAMILY:IPR004090 , InterPro:IN-FAMILY:IPR004091 , PDB:Structure:2ASR , PDB:Structure:2L9G , 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

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Genetic Regulation Schematic: ?

Genetic regulation schematic for tar

GO Terms:

Biological Process: GO:0006935 - chemotaxis Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01a, Silverman77]
GO:0007165 - signal transduction Inferred by computational analysis [UniProtGOA11a, GOA01a]
Molecular Function: GO:0004871 - signal transducer activity Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01a, Springer77]
GO:0004888 - transmembrane signaling receptor activity Inferred from experiment Inferred by computational analysis [GOA01a, Springer77]
GO:0005515 - protein binding Inferred from experiment [Arifuzzaman06, Rajagopala09]
GO:0043424 - protein histidine kinase binding Inferred from experiment [Gegner92]
Cellular Component: GO:0005887 - integral component of plasma membrane Inferred by computational analysis Inferred from experiment [Ridgway77, Krikos83, Lynch91]
GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a, GOA01a]

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

Essentiality data for tar 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]

Created 13-Nov-2013 by Mackie A , Macquarie University

Subunit of: chemotaxis signaling complex - aspartate sensing

Synonyms: MCP-II signaling complex

Subunit composition of chemotaxis signaling complex - aspartate sensing = [(CheA)2][CheW]2[(Tar)2]3
         CheA(L) histidine kinase = (CheA)2
         methyl accepting chemotaxis protein Tar = (Tar)2 (extended summary available)

The tar gene product is one of four methyl-accepting chemotaxis proteins (MCPs) in E. coli. MCP-II is the receptor for the attractant L-aspartate and related amino acids and dicarboxylic acids. MCP-II also interacts with the periplasmic maltose-binding protein to mediate taxis to the attractant maltose. It also responds to the repellents cobalt and nickel and is thermosensitive. [Nara96, Gardina97, Gardina92, Krikos83, Wang80, Chi97, Hoch95, Neidhardt96, Salman07, Jiang09, Wheatley15].

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 (reviewed in [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 (reviewed in [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 [Barak92]. 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 [Li00].

Reviews: [Stock00, Hazelbauer08, Sourjik04, Sourjik10]

Citations: [Neumann10]

Sequence Features

Protein sequence of Tar with features indicated

Feature Class Location Citations Comment
Transmembrane-Region 7 -> 33
UniProt: Helical;; Non-Experimental Qualifier: potential;
Protein-Segment 64 -> 73
UniProt: The 3 Arg may form a positively charged pocket, which binds the alpha-carboxyl group of the attractant AA; Sequence Annotation Type: region of interest;
Sequence-Conflict 164
[Krikos83, UniProt10a]
UniProt: (in Ref. 1; AAA23566);
Transmembrane-Region 191 -> 211
UniProt: Helical;; Non-Experimental Qualifier: potential;
Conserved-Region 214 -> 266
UniProt: HAMP;
Conserved-Region 271 -> 500
UniProt: Methyl-accepting transducer;
Glutamate-methyl-ester-Modification 295
UniProt: Glutamate methyl ester (Gln).
Glutamate-methyl-ester-Modification 302
UniProt: Glutamate methyl ester (Glu).
Glutamate-methyl-ester-Modification 309
UniProt: Glutamate methyl ester (Gln).
Glutamate-methyl-ester-Modification 491
UniProt: Glutamate methyl ester (Glu).
Glutamate-methyl-ester-Modification 500
UniProt: Glutamate methyl ester (Glu).

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Unit:

Transcription-unit diagram


10/20/97 Gene b1886 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10988; confirmed by SwissProt match.


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

Ames08: Ames P, Zhou Q, Parkinson JS (2008). "Mutational Analysis of the Connector Segment in the HAMP Domain of Tsr, the E. coli Serine Chemoreceptor." J Bacteriol NIL. PMID: 18621896

Ames13: Ames P, Zhou Q, Parkinson JS (2013). "HAMP domain structural determinants for signalling and sensory adaptation in Tsr, the Escherichia coli serine chemoreceptor." Mol Microbiol. PMID: 24205875

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

Arnosti89: Arnosti DN, Chamberlin MJ (1989). "Secondary sigma factor controls transcription of flagellar and chemotaxis genes in Escherichia coli." Proc Natl Acad Sci U S A 86(3);830-4. PMID: 2644646

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

Barak92: 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

Bi13a: Bi S, Yu D, Si G, Luo C, Li T, Ouyang Q, Jakovljevic V, Sourjik V, Tu Y, Lai L (2013). "Discovery of novel chemoeffectors and rational design of Escherichia coli chemoreceptor specificity." Proc Natl Acad Sci U S A 110(42);16814-9. PMID: 24082101

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

Bowie95: Bowie JU, Pakula AA, Simon MI (1995). "The three-dimensional structure of the aspartate receptor from Escherichia coli." Acta Crystallogr D Biol Crystallogr 51(Pt 2);145-54. PMID: 15299315

Boyd80: Boyd A, Simon MI (1980). "Multiple electrophoretic forms of methyl-accepting chemotaxis proteins generated by stimulus-elicited methylation in Escherichia coli." J Bacteriol 143(2);809-15. PMID: 6782079

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

Chelsky80: Chelsky D, Dahlquist FW (1980). "Structural studies of methyl-accepting chemotaxis proteins of Escherichia coli: evidence for multiple methylation sites." Proc Natl Acad Sci U S A 77(5);2434-8. PMID: 6994098

Chi97: Chi YI, Yokota H, Kim SH (1997). "Apo structure of the ligand-binding domain of aspartate receptor from Escherichia coli and its comparison with ligand-bound or pseudoligand-bound structures." FEBS Lett 1997;414(2);327-32. PMID: 9315712

Cochran96: Cochran AG, Kim PS (1996). "Imitation of Escherichia coli aspartate receptor signaling in engineered dimers of the cytoplasmic domain." Science 271(5252);1113-6. PMID: 8599087

DeFranco80: DeFranco AL, Koshland DE (1980). "Multiple methylation in processing of sensory signals during bacterial chemotaxis." Proc Natl Acad Sci U S A 77(5);2429-33. PMID: 6446711

Draheim05: Draheim RR, Bormans AF, Lai RZ, Manson MD (2005). "Tryptophan residues flanking the second transmembrane helix (TM2) set the signaling state of the Tar chemoreceptor." Biochemistry 44(4);1268-77. PMID: 15667220

Engstrom80: Engstrom P, Hazelbauer GL (1980). "Multiple methylation of methyl-accepting chemotaxis proteins during adaptation of E. coli to chemical stimuli." Cell 20(1);165-71. PMID: 6993007

Falke87: Falke JJ, Koshland DE (1987). "Global flexibility in a sensory receptor: a site-directed cross-linking approach." Science 237(4822);1596-600. PMID: 2820061

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

Gardina92: Gardina P, Conway C, Kossman M, Manson M (1992). "Aspartate and maltose-binding protein interact with adjacent sites in the Tar chemotactic signal transducer of Escherichia coli." J Bacteriol 1992;174(5);1528-36. PMID: 1537797

Gardina96: Gardina PJ, Manson MD (1996). "Attractant signaling by an aspartate chemoreceptor dimer with a single cytoplasmic domain." Science 274(5286);425-6. PMID: 8832892

Gardina97: Gardina PJ, Bormans AF, Hawkins MA, Meeker JW, Manson MD (1997). "Maltose-binding protein interacts simultaneously and asymmetrically with both subunits of the Tar chemoreceptor." Mol Microbiol 1997;23(6);1181-91. PMID: 9106209

Gardina98: Gardina PJ, Bormans AF, Manson MD (1998). "A mechanism for simultaneous sensing of aspartate and maltose by the Tar chemoreceptor of Escherichia coli." Mol Microbiol 29(5);1147-54. PMID: 9767583

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

Gerstein99: Gerstein M, Chothia C (1999). "Perspectives: signal transduction. Proteins in motion." Science 285(5434);1682-3. PMID: 10523185

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

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

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

Hedblom83: Hedblom ML, Adler J (1983). "Chemotactic response of Escherichia coli to chemically synthesized amino acids." J Bacteriol 155(3);1463-6. PMID: 6350273

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

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

Imae87: Imae Y, Oosawa K, Mizuno T, Kihara M, Macnab RM (1987). "Phenol: a complex chemoeffector in bacterial chemotaxis." J Bacteriol 169(1);371-9. PMID: 3025180

Jiang09: Jiang L, Ouyang Q, Tu Y (2009). "A mechanism for precision-sensing via a gradient-sensing pathway: a model of Escherichia coli thermotaxis." Biophys J 97(1);74-82. PMID: 19580745

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

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

Krikos85: Krikos A, Conley MP, Boyd A, Berg HC, Simon MI (1985). "Chimeric chemosensory transducers of Escherichia coli." Proc Natl Acad Sci U S A 82(5);1326-30. PMID: 3883356

Kundu97: Kundu TK, Kusano S, Ishihama A (1997). "Promoter selectivity of Escherichia coli RNA polymerase sigmaF holoenzyme involved in transcription of flagellar and chemotaxis genes." J Bacteriol 179(13);4264-9. PMID: 9209042

Lai08: Lai RZ, Bormans AF, Draheim RR, Wright GA, Manson MD (2008). "The region preceding the C-terminal NWETF pentapeptide modulates baseline activity and aspartate inhibition of Escherichia coli Tar." Biochemistry 47(50);13287-95. PMID: 19053273

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

Li00: 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

Lynch91: Lynch BA, Koshland DE (1991). "Disulfide cross-linking studies of the transmembrane regions of the aspartate sensory receptor of Escherichia coli." Proc Natl Acad Sci U S A 88(23);10402-6. PMID: 1660136

Manson09: Manson MD (2009). "A mutational wrench in the HAMP gearbox." Mol Microbiol 73(5);742-6. PMID: 19678895

Manson11: Manson MD (2011). "Not too loose, not too tight--just right. Biphasic control of the Tsr HAMP domain." Mol Microbiol 80(3);573-6. PMID: 21355897

Manson85: Manson MD, Boos W, Bassford PJ, Rasmussen BA (1985). "Dependence of maltose transport and chemotaxis on the amount of maltose-binding protein." J Biol Chem 260(17);9727-33. PMID: 3894359

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

Mesibov72: Mesibov R, Adler J (1972). "Chemotaxis toward amino acids in Escherichia coli." J Bacteriol 112(1);315-26. PMID: 4562400

Mise14: Mise T, Matsunami H, Samatey FA, Maruyama IN (2014). "Crystallization and preliminary X-ray diffraction analysis of the periplasmic domain of the Escherichia coli aspartate receptor Tar and its complex with aspartate." Acta Crystallogr F Struct Biol Commun 70(Pt 9);1219-23. PMID: 25195895

Mowbray87: Mowbray SL, Koshland DE (1987). "Additive and independent responses in a single receptor: aspartate and maltose stimuli on the tar protein." Cell 50(2);171-80. PMID: 3297352

Nara96: Nara T, Kawagishi I, Nishiyama S, Homma M, Imae Y (1996). "Modulation of the thermosensing profile of the Escherichia coli aspartate receptor tar by covalent modification of its methyl-accepting sites." J Biol Chem 1996;271(30);17932-6. PMID: 8663384

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.

Neumann10: Neumann S, Hansen CH, Wingreen NS, Sourjik V (2010). "Differences in signalling by directly and indirectly binding ligands in bacterial chemotaxis." EMBO J 29(20);3484-95. PMID: 20834231

Nishiyama99: Nishiyama S, Maruyama IN, Homma M, Kawagishi I (1999). "Inversion of thermosensing property of the bacterial receptor Tar by mutations in the second transmembrane region." J Mol Biol 286(5);1275-84. PMID: 10064695

Ottemann99: Ottemann KM, Xiao W, Shin YK, Koshland DE (1999). "A piston model for transmembrane signaling of the aspartate receptor." Science 285(5434);1751-4. PMID: 10481014

Pakula92: Pakula AA, Simon MI (1992). "Determination of transmembrane protein structure by disulfide cross-linking: the Escherichia coli Tar receptor." Proc Natl Acad Sci U S A 89(9);4144-8. PMID: 1315053

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

Parkinson78: Parkinson JS (1978). "Complementation analysis and deletion mapping of Escherichia coli mutants defective in chemotaxis." J Bacteriol 135(1);45-53. PMID: 353036

Parkinson82: Parkinson JS, Houts SE (1982). "Isolation and behavior of Escherichia coli deletion mutants lacking chemotaxis functions." J Bacteriol 151(1);106-13. PMID: 7045071

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

Reader79: Reader RW, Tso WW, Springer MS, Goy MF, Adler J (1979). "Pleiotropic aspartate taxis and serine taxis mutants of Escherichia coli." J Gen Microbiol 111(2);363-74. PMID: 383889

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

Salman07: Salman H, Libchaber A (2007). "A concentration-dependent switch in the bacterial response to temperature." Nat Cell Biol 9(9);1098-100. PMID: 17694049

Samanta15: Samanta D, Borbat PP, Dzikovski B, Freed JH, Crane BR (2015). "Bacterial chemoreceptor dynamics correlate with activity state and are coupled over long distances." Proc Natl Acad Sci U S A 112(8);2455-60. PMID: 25675479

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

Silverman77: Silverman M, Simon M (1977). "Chemotaxis in Escherichia coli: methylation of che gene products." Proc Natl Acad Sci U S A 74(8);3317-21. PMID: 333434

Slocum83: Slocum MK, Parkinson JS (1983). "Genetics of methyl-accepting chemotaxis proteins in Escherichia coli: organization of the tar region." J Bacteriol 155(2);565-77. PMID: 6307970

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

Sourjik04: Sourjik V (2004). "Receptor clustering and signal processing in E. coli chemotaxis." Trends Microbiol 12(12);569-76. PMID: 15539117

Sourjik10: Sourjik V, Armitage JP (2010). "Spatial organization in bacterial chemotaxis." EMBO J 29(16);2724-33. PMID: 20717142

Springer77: Springer MS, Goy MF, Adler J (1977). "Sensory transduction in Escherichia coli: two complementary pathways of information processing that involve methylated proteins." Proc Natl Acad Sci U S A 74(8);3312-6. PMID: 333433

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

Stock96: Stock J (1996). "Signaling across membranes: a one and a two and a." Science 274(5286);370-1. PMID: 8927993

Stoddard92: Stoddard BL, Bui JD, Koshland DE (1992). "Structure and dynamics of transmembrane signaling by the Escherichia coli aspartate receptor." Biochemistry 31(48);11978-83. PMID: 1457398

Tatsuno96: Tatsuno I, Homma M, Oosawa K, Kawagishi I (1996). "Signaling by the Escherichia coli aspartate chemoreceptor Tar with a single cytoplasmic domain per dimer." Science 274(5286);423-5. PMID: 8832891

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

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt15: UniProt Consortium (2015). "UniProt version 2015-01 released on 2015-01-16 00:00:00." Database.

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

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

Wang80: Wang EA, Koshland DE (1980). "Receptor structure in the bacterial sensing system." Proc Natl Acad Sci U S A 1980;77(12);7157-61. PMID: 6784119

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

Wheatley15: Wheatley RW, Juers DH, Lev BB, Huber RE, Noskov SY (2015). "Elucidating factors important for monovalent cation selectivity in enzymes: E. coli β-galactosidase as a model." Phys Chem Chem Phys 17(16);10899-909. PMID: 25820412

Wolff88: Wolff C, Parkinson JS (1988). "Aspartate taxis mutants of the Escherichia coli tar chemoreceptor." J Bacteriol 170(10);4509-15. PMID: 3049535

Wright11: Wright GA, Crowder RL, Draheim RR, Manson MD (2011). "Mutational analysis of the transmembrane helix 2-HAMP domain connection in the Escherichia coli aspartate chemoreceptor tar." J Bacteriol 193(1);82-90. PMID: 20870768

Yang15: Yang Y, Pollard A, Hofler C, Poschet G, Wirtz M, Hell R, Sourjik V (2015). "Relation between chemotaxis and consumption of amino acids in bacteria." Mol Microbiol. PMID: 25807888

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

Zhang99: Zhang Y, Gardina PJ, Kuebler AS, Kang HS, Christopher JA, Manson MD (1999). "Model of maltose-binding protein/chemoreceptor complex supports intrasubunit signaling mechanism." Proc Natl Acad Sci U S A 96(3);939-44. PMID: 9927672

Zhou09: Zhou Q, Ames P, Parkinson JS (2009). "Mutational analyses of HAMP helices suggest a dynamic bundle model of input-output signalling in chemoreceptors." Mol Microbiol 73(5);801-14. PMID: 19656294

Zhou11: Zhou Q, Ames P, Parkinson JS (2011). "Biphasic control logic of HAMP domain signalling in the Escherichia coli serine chemoreceptor." Mol Microbiol 80(3);596-611. PMID: 21306449

Other References Related to Gene Regulation

Constantinidou06: Constantinidou C, Hobman JL, Griffiths L, Patel MD, Penn CW, Cole JA, Overton TW (2006). "A reassessment of the FNR regulon and transcriptomic analysis of the effects of nitrate, nitrite, NarXL, and NarQP as Escherichia coli K12 adapts from aerobic to anaerobic growth." J Biol Chem 281(8);4802-15. PMID: 16377617

Helmann87: Helmann JD, Chamberlin MJ (1987). "DNA sequence analysis suggests that expression of flagellar and chemotaxis genes in Escherichia coli and Salmonella typhimurium is controlled by an alternative sigma factor." Proc Natl Acad Sci U S A 84(18);6422-4. PMID: 3306678

Ide99: Ide N, Ikebe T, Kutsukake K (1999). "Reevaluation of the promoter structure of the class 3 flagellar operons of Escherichia coli and Salmonella." Genes Genet Syst 74(3);113-6. PMID: 10586520

Ko00a: Ko M, Park C (2000). "Two novel flagellar components and H-NS are involved in the motor function of Escherichia coli." J Mol Biol 303(3);371-82. PMID: 11031114

Liu95: Liu X, Matsumura P (1995). "An alternative sigma factor controls transcription of flagellar class-III operons in Escherichia coli: gene sequence, overproduction, purification and characterization." Gene 164(1);81-4. PMID: 7590326

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 19.0 on Fri Oct 9, 2015, BIOCYC14B.