Recombinant Escherichia coli Methyl-accepting chemotaxis protein II (tar), partial

1. Thus, the proportion of polypeptide chain that is locally and presumably transiently disordered is a structural feature of cytoplasmic domain dynamics that varies with functional region and modification-induced signaling state. PMID: 27318193
2. There is a differential repositioning of the second transmembrane helices from E. coli Tar and EnvZ upon moving the flanking aromatic residues. PMID: 25445668
3. the Tar(FO) modules demonstrate that trimerized signaling tips self-associate, bind CheA and CheW, and facilitate conversion of CheA to an active conformation. PMID: 25967982
4. Residues at the cytoplasmic end of transmembrane helix 2 determine the signal output of the Tar chemoreceptor. PMID: 23495653
5. Such inversion is enabled by opposing pH sensing by the two major chemoreceptors, Tar and Tsr, such that the relative strength of the response is modulated by adaptive receptor methylation. PMID: 23078189
6. Here we report the overexpression system for aCB2 in Escherichia coli C43(DE3) facilitated by two fusion partners: Mistic and TarCF, a C-terminal fragment of the bacterial chemosensory transducer Tar at the C-terminal of the CB2 open reading frame region. PMID: 22406258
7. characterization of structural features of carboxyl-terminal 40 residues of Tar; identifed carboxyl-terminal linker between receptor body and the pentapeptide is an unstructured, disordered segment that can serve as a flexible arm and enzyme tether PMID: 21858888
8. Ligand specificity is determined by differentially arranged common ligand-binding residues in bacterial amino acid chemoreceptors Tsr and Tar PMID: 21979954
9. Tar molecules with the cytoplasmic methylation and kinase control domains of Tsr still sensed phenol as an attractant. PMID: 21965561
10. The cytoplasmic domains of Tar and Tsr receptors are close to each other near the trimer contact region at the cytoplasmic tip. PMID: 21174433
11. These results with Tar-EnvZ hybrid receptor mutants suggest that intersubunit interactions in the HAMP linker normally mediate signal transduction through both subunits in a sensor dimer. PMID: 15316026
12. mutations in the protein motifs of Tar significantly reduced the ability of the transmembrane domains to dimerize PMID: 15330757
13. The tryptophan residues flanking the second transmembrane helix of Tar, especially Trp-209, are crucial in setting the baseline activity and ligand sensitivity of this chemoreceptor. PMID: 15667220
14. assisted adaptational modification (methylation, demthylation and deamidation) in vitro of Trg chemorecptor PMID: 15916610
15. polar localization of Tar fused to green fluorescent protein is influenced by its own amidation (methylation) state and the expression of another chemoreceptor (Tsr) PMID: 16267289
16. Data show that Tar can be readily mutated to respond to new chemical signals, but that the overall change in specificity depends on the target compound. PMID: 16359703
17. The pentapeptide linker in Tar is important for chemotaxis because of its role in adaptational modification. PMID: 16573695
18. The fundamental mechanism of transmembrane signaling is conserved between homodimeric sensor kinases (with NarX) and chemoreceptors. PMID: 16707686
19. Data suggest that Tar()-Tsr* suppression most likely occurs through compensatory changes in the conformation or dynamics of a mixed receptor signaling complex, presumably based on trimer-of-dimer interactions. PMID: 16751275
20. The organization of these receptor/signaling complexes is determined by conserved interactions between the constituent chemotaxis proteins and may represent the active form in vivo. PMID: 16973743
21. A mutational analysis of Tar residues 505-548 reveals that the more of this region is deleted, the less sensitive Tar is to inhibition by aspartate. PMID: 19053273

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KEGG: ecj:JW1875

STRING: 316385.ECDH10B_2027