Home LiteratureArticle Details
PMID: 11295559 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S. Review

Transmembrane signaling in bacterial chemoreceptors.

Trends in biochemical sciences ·Vol. 26 ·No. 4 ·2001-04-00 ·Pages 257-65

Falke JJ, Hazelbauer GL

Abstract

Bacterial chemoreceptors mediate chemotaxis by recognizing specific chemicals and regulating a noncovalently associated histidine kinase. Ligand binding to the external domain of the membrane-spanning receptor generates a transmembrane signal that modulates kinase activity inside the cell. This transmembrane signaling is being investigated by novel strategies, which have revealed a remarkably subtle conformational signal carried by a signaling helix that spans the entire length of the >350-A-long receptor. Multiple, independent lines of evidence indicate that, in the periplasmic and transmembrane domains, conformational signaling is a piston-type sliding of the signaling helix towards the cytoplasm.

MeSH Terms
Bacteria/metabolism Bacterial Proteins Cell Membrane/metabolism Chemoreceptor Cells/metabolism Signal Transduction
Chemicals
Bacterial Proteins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Falke J J
Department of Chemistry and Biochemistry, University of Colorado, 80309-0215, Boulder, CO, USA. falke@colorado.edu
Hazelbauer G L
References (55)
55 references, click to expand
  1. Covalent modification regulates ligand binding to receptor complexes in the chemosensory system of Escherichia coli.
    Cell. 2000 Feb 4;100(3):357-65 PMID: 10676817
  2. Efficient adaptational demethylation of chemoreceptors requires the same enzyme-docking site as efficient methylation.
    Proc Natl Acad Sci U S A. 1999 Sep 14;96(19):10667-72 PMID: 10485883
  3. PAS domain residues involved in signal transduction by the Aer redox sensor of Escherichia coli.
    Mol Microbiol. 2000 May;36(4):806-16 PMID: 10844669
  4. Attractant regulation of the aspartate receptor-kinase complex: limited cooperative interactions between receptors and effects of the receptor modification state.
    Biochemistry. 2000 Aug 8;39(31):9486-93 PMID: 10924144
  5. A tale of two components: a novel kinase and a regulatory switch.
    Nat Struct Biol. 2000 Aug;7(8):626-33 PMID: 10932244
  6. Molecular model of a lattice of signalling proteins involved in bacterial chemotaxis.
    Nat Cell Biol. 2000 Nov;2(11):792-6 PMID: 11056533
  7. Site-directed solid-state NMR measurement of a ligand-induced conformational change in the serine bacterial chemoreceptor.
    Biochemistry. 2001 Feb 6;40(5):1358-66 PMID: 11170463
  8. Mutations that affect ligand binding to the Escherichia coli aspartate receptor: implications for transmembrane signaling.
    J Biol Chem. 2001 Jan 26;276(4):2808-15 PMID: 11042221
  9. Signalling substitutions in the periplasmic domain of chemoreceptor Trg induce or reduce helical sliding in the transmembrane domain.
    Mol Microbiol. 2001 May;40(4):824-34 PMID: 11401690
  10. Global flexibility in a sensory receptor: a site-directed cross-linking approach.
    Science. 1987 Sep 25;237(4822):1596-600 PMID: 2820061
  11. Site-directed cross-linking. Establishing the dimeric structure of the aspartate receptor of bacterial chemotaxis.
    J Biol Chem. 1988 May 5;263(13):6268-75 PMID: 2834370
  12. Reconstitution of the bacterial chemotaxis signal transduction system from purified components.
    J Biol Chem. 1991 May 25;266(15):9764-70 PMID: 1851755
  13. Genetic evidence for interaction between the CheW and Tsr proteins during chemoreceptor signaling by Escherichia coli.
    J Bacteriol. 1991 Aug;173(16):4941-51 PMID: 1860813
  14. Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand.
    Science. 1991 Nov 29;254(5036):1342-7 PMID: 1660187
  15. Determination of transmembrane protein structure by disulfide cross-linking: the Escherichia coli Tar receptor.
    Proc Natl Acad Sci U S A. 1992 May 1;89(9):4144-8 PMID: 1315053
  16. Attenuation of sensory receptor signaling by covalent modification.
    Proc Natl Acad Sci U S A. 1992 Aug 1;89(15):6756-60 PMID: 1495964
  17. Thermal motions of surface alpha-helices in the D-galactose chemosensory receptor. Detection by disulfide trapping.
    J Mol Biol. 1992 Aug 20;226(4):1219-35 PMID: 1518053
  18. Ligand occupancy mimicked by single residue substitutions in a receptor: transmembrane signaling induced by mutation.
    Proc Natl Acad Sci U S A. 1992 Sep 1;89(17):7890-4 PMID: 1518809
  19. Polar location of the chemoreceptor complex in the Escherichia coli cell.
    Science. 1993 Mar 19;259(5102):1717-23 PMID: 8456299
  20. Ligand binding induces an asymmetrical transmembrane signal through a receptor dimer.
    J Mol Biol. 1993 Jul 20;232(2):493-8 PMID: 8393938
  21. Aspartate receptors of Escherichia coli and Salmonella typhimurium bind ligand with negative and half-of-the-sites cooperativity.
    Biochemistry. 1994 Jan 25;33(3):629-34 PMID: 8292590
  22. Attractant- and disulfide-induced conformational changes in the ligand binding domain of the chemotaxis aspartate receptor: a 19F NMR study.
    Biochemistry. 1994 May 24;33(20):6100-9 PMID: 7910759
  23. "Frozen" dynamic dimer model for transmembrane signaling in bacterial chemotaxis receptors.
    Protein Sci. 1994 Feb;3(2):159-65 PMID: 8003953
  24. Deducing the organization of a transmembrane domain by disulfide cross-linking. The bacterial chemoreceptor Trg.
    J Biol Chem. 1994 Nov 25;269(47):29920-7 PMID: 7961989
  25. Transmembrane signalling and the aspartate receptor.
    Structure. 1994 Sep 15;2(9):877-87 PMID: 7812719
  26. Transmembrane signaling characterized in bacterial chemoreceptors by using sulfhydryl cross-linking in vivo.
    Proc Natl Acad Sci U S A. 1995 Apr 11;92(8):3391-5 PMID: 7724572
  27. Identification of functionally important helical faces in transmembrane segments by scanning mutagenesis.
    Proc Natl Acad Sci U S A. 1995 Jun 6;92(12):5416-20 PMID: 7777522
  28. Transmembrane signaling by the aspartate receptor: engineered disulfides reveal static regions of the subunit interface.
    Biochemistry. 1995 Aug 1;34(30):9722-33 PMID: 7626643
  29. Lock on/off disulfides identify the transmembrane signaling helix of the aspartate receptor.
    J Biol Chem. 1995 Oct 13;270(41):24043-53 PMID: 7592603
  30. A model for transmembrane signalling by the aspartate receptor based on random-cassette mutagenesis and site-directed disulfide cross-linking.
    J Mol Biol. 1995 Nov 3;253(4):530-46 PMID: 7473732
  31. How bacteria sense and swim.
    Annu Rev Microbiol. 1995;49:489-522 PMID: 8561469
  32. Imitation of Escherichia coli aspartate receptor signaling in engineered dimers of the cytoplasmic domain.
    Science. 1996 Feb 23;271(5252):1113-6 PMID: 8599087
  33. Molecular mechanism of transmembrane signaling by the aspartate receptor: a model.
    Proc Natl Acad Sci U S A. 1996 Mar 19;93(6):2545-50 PMID: 8637911
  34. The receptor binding site for the methyltransferase of bacterial chemotaxis is distinct from the sites of methylation.
    Biochemistry. 1996 Apr 16;35(15):4984-93 PMID: 8664291
  35. Methylation segments are not required for chemotactic signalling by cytoplasmic fragments of Tsr, the methyl-accepting serine chemoreceptor of Escherichia coli.
    Mol Microbiol. 1996 Feb;19(4):737-46 PMID: 8820644
  36. Signaling by the Escherichia coli aspartate chemoreceptor Tar with a single cytoplasmic domain per dimer.
    Science. 1996 Oct 18;274(5286):423-5 PMID: 8832891
  37. Attractant signaling by an aspartate chemoreceptor dimer with a single cytoplasmic domain.
    Science. 1996 Oct 18;274(5286):425-6 PMID: 8832892
  38. 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. 1996 Oct 15;93(21):11546-51 PMID: 8876172
  39. The serine chemoreceptor from Escherichia coli is methylated through an inter-dimer process.
    Biochemistry. 1997 Sep 30;36(39):11851-7 PMID: 9305977
  40. 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 Sep 8;414(2):327-32 PMID: 9315712
  41. Methylation of the Escherichia coli chemotaxis receptors: intra- and interdimer mechanisms.
    Biochemistry. 1997 Oct 28;36(43):13441-8 PMID: 9341238
  42. High- and low-abundance chemoreceptors in Escherichia coli: differential activities associated with closely related cytoplasmic domains.
    J Bacteriol. 1997 Nov;179(21):6714-20 PMID: 9352921
  43. Receptor-mediated protein kinase activation and the mechanism of transmembrane signaling in bacterial chemotaxis.
    EMBO J. 1997 Dec 15;16(24):7231-40 PMID: 9405352
  44. Cysteine and disulfide scanning reveals a regulatory alpha-helix in the cytoplasmic domain of the aspartate receptor.
    J Biol Chem. 1997 Dec 26;272(52):32878-88 PMID: 9407066
  45. 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. 1997;13:457-512 PMID: 9442881
  46. Cysteine and disulfide scanning reveals two amphiphilic helices in the linker region of the aspartate chemoreceptor.
    Biochemistry. 1998 Jul 28;37(30):10746-56 PMID: 9692965
  47. Identification of a site critical for kinase regulation on the central processing unit (CPU) helix of the aspartate receptor.
    Biochemistry. 1999 Jan 5;38(1):329-36 PMID: 9890914
  48. Model of maltose-binding protein/chemoreceptor complex supports intrasubunit signaling mechanism.
    Proc Natl Acad Sci U S A. 1999 Feb 2;96(3):939-44 PMID: 9927672
  49. Structural analysis of bacterial chemotaxis proteins: components of a dynamic signaling system.
    J Struct Biol. 1998 Dec 15;124(2-3):189-200 PMID: 10049806
  50. Signaling domain of the aspartate receptor is a helical hairpin with a localized kinase docking surface: cysteine and disulfide scanning studies.
    Biochemistry. 1999 Jul 20;38(29):9317-27 PMID: 10413506
  51. The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteins.
    FEMS Microbiol Lett. 1999 Jul 1;176(1):111-6 PMID: 10418137
  52. The aspartate receptor cytoplasmic domain: in situ chemical analysis of structure, mechanism and dynamics.
    Structure. 1999 Jul 15;7(7):829-40 PMID: 10425684
  53. Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor.
    Nature. 1999 Aug 19;400(6746):787-92 PMID: 10466731
  54. A piston model for transmembrane signaling of the aspartate receptor.
    Science. 1999 Sep 10;285(5434):1751-4 PMID: 10481014
  55. Domain organization and flavin adenine dinucleotide-binding determinants in the aerotaxis signal transducer Aer of Escherichia coli.
    Proc Natl Acad Sci U S A. 2000 May 23;97(11):5830-5 PMID: 10811894
Article Info
Journal
Trends in biochemical sciences
Abbr.
Trends Biochem Sci
ISSN
0968-0004
DOI
10.1016/s0968-0004(00)01770-9
Email
falke@colorado.edu
Published
2001-04-00
Pages
257-65
Language
English
Region
England
NLM ID
7610674
PMCID
PMC2895674
Subset
IM
Grants
NIGMS NIH HHS · R01 GM040731 · United States
NIGMS NIH HHS · R01 GM029963 · United States
NIGMS NIH HHS · R37 GM029963 · United States
NIGMS NIH HHS · R01 GM040731-14 · United States
NIGMS NIH HHS · GM29963 · United States
NIGMS NIH HHS · GM40731 · United States
External Links
PubMed source DOI: 10.1016/s0968-0004(00)01770-9 PMC Full Text View journal details
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com

Copyright © 2026.Genelibs Jinan Honghui Biotechnology Co., Ltd. 鲁ICP备20007159号-2