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PMID: 7882970 Published · ppublish English Comparative Study Journal Article

Chemotaxis and phototaxis require a CheA histidine kinase in the archaeon Halobacterium salinarium.

The EMBO journal ·Vol. 14 ·No. 4 ·1995-02-15 ·Pages 667-73

Rudolph J, Oesterhelt D

Abstract

Histidine kinases are part of the two-component signal transduction system responsible for eubacterial responses to diverse environmental signals. They have recently been detected in eukaryotes but their existence in the kingdom Archaea remains uncertain. Here we report the sequence and function of a histidine kinase (CheAH.s.) from Halobacterium salinarium, the first such transmitter in Archaea. The protein CheAH.s. (668 residues) has significant sequence identity with the CheA proteins known from eubacterial signal transduction (e.g. 34% identity with CheA from Bacillus subtilis). Antibodies were raised against CheAH.s. as expressed in Escherichia coli and were used in Western blotting to demonstrate the expression of cheAH.s. in H. salinarium. As has been observed for other halophilic proteins, CheAH.s. has a deviant electrophoretic migration, with an apparent molecular weight of 103 kDa on SDS-PAGE compared with a calculated molecular weight of 72 kDa. Deletion of a part of the cheAH.s. gene leads to loss of both chemotactic and phototactic responses in H. salinarium as measured by swarm plate assays, motion analysis and tethering experiments. This indicates that CheAH.s. plays a crucial role in chemical and light signal integration, presumably interacting with at least two phototransducers and a number of chemoreceptors.

Related Genes
cheA
MeSH Terms
Amino Acid Sequence Bacterial Proteins Base Sequence Chemotaxis Escherichia coli/genetics Escherichia coli Proteins Gene Expression Genes, Bacterial Halobacterium/physiology Histidine Kinase Light Membrane Proteins/physiology Methyl-Accepting Chemotaxis Proteins Molecular Sequence Data Photoreceptor Cells/physiology Protein Kinases/physiology Recombinant Proteins Sequence Alignment Sequence Homology, Amino Acid Signal Transduction
Chemicals
Bacterial Proteins Escherichia coli Proteins Membrane Proteins Methyl-Accepting Chemotaxis Proteins Recombinant Proteins Protein Kinases Histidine Kinase cheA protein, E coli
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Rudolph J
Max Planck Institute for Biochemistry, Martinsried, Germany.
Oesterhelt D
References (45)
45 references, click to expand
  1. Two photosystems controlling behavioural responses of Halobacterium halobium.
    Nature. 1975 Sep 4;257(5521):46-8 PMID: 1161001
  2. Mevinolin-resistant mutations identify a promoter and the gene for a eukaryote-like 3-hydroxy-3-methylglutaryl-coenzyme A reductase in the archaebacterium Haloferax volcanii.
    J Biol Chem. 1992 Mar 25;267(9):5829-34 PMID: 1556098
  3. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.
    Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350-4 PMID: 388439
  4. Chemosensory responses of Halobacterium halobium.
    J Bacteriol. 1979 Dec;140(3):749-53 PMID: 533767
  5. The 3'-terminal nucleotide sequence of the Halobacterium halobium 16 S rRNA.
    FEBS Lett. 1982 Jul 19;144(1):177-80 PMID: 7106297
  6. Morphology, function and isolation of halobacterial flagella.
    J Mol Biol. 1984 Jul 15;176(4):459-75 PMID: 6748081
  7. Mechanism of colour discrimination by a bacterial sensory rhodopsin.
    Nature. 1984 Dec 6-12;312(5994):509-13 PMID: 6504161
  8. A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes.
    Proc Natl Acad Sci U S A. 1985 Feb;82(4):1074-8 PMID: 3156376
  9. Integration of photosensory signals in Halobacterium halobium.
    J Bacteriol. 1986 Jul;167(1):305-11 PMID: 3722125
  10. Signal formation in the halobacterial photophobic response mediated by a fourth retinal protein (P480).
    J Mol Biol. 1987 May 20;195(2):333-42 PMID: 3656416
  11. Protein phosphorylation is involved in bacterial chemotaxis.
    Proc Natl Acad Sci U S A. 1987 Nov;84(21):7609-13 PMID: 3313398
  12. CheA protein, a central regulator of bacterial chemotaxis, belongs to a family of proteins that control gene expression in response to changing environmental conditions.
    Proc Natl Acad Sci U S A. 1988 Mar;85(5):1403-7 PMID: 3278311
  13. Cloning of the C-terminal cytoplasmic fragment of the tar protein and effects of the fragment on chemotaxis of Escherichia coli.
    J Bacteriol. 1988 Jun;170(6):2521-6 PMID: 3286610
  14. Methyl-accepting protein associated with bacterial sensory rhodopsin I.
    J Bacteriol. 1988 Sep;170(9):4280-5 PMID: 3410829
  15. The methyl-accepting transducer protein HtrI is functionally associated with the photoreceptor sensory rhodopsin I in the archaeon Halobacterium salinarium.
    EMBO J. 1993 Aug;12(8):2999-3005 PMID: 8344242
  16. Assembly and function of a quaternary signal transduction complex monitored by surface plasmon resonance.
    Nature. 1993 Sep 23;365(6444):343-7 PMID: 8377825
  17. Bacteriorhodopsin is involved in halobacterial photoreception.
    Proc Natl Acad Sci U S A. 1993 Oct 15;90(20):9446-50 PMID: 8415720
  18. Arabidopsis ethylene-response gene ETR1: similarity of product to two-component regulators.
    Science. 1993 Oct 22;262(5133):539-44 PMID: 8211181
  19. A yeast protein similar to bacterial two-component regulators.
    Science. 1993 Oct 22;262(5133):566-9 PMID: 8211183
  20. Assembly of an MCP receptor, CheW, and kinase CheA complex in the bacterial chemotaxis signal transduction pathway.
    Cell. 1992 Sep 18;70(6):975-82 PMID: 1326408
  21. Primary structure of an archaebacterial transducer, a methyl-accepting protein associated with sensory rhodopsin I.
    Proc Natl Acad Sci U S A. 1992 Dec 15;89(24):11915-9 PMID: 1465418
  22. Communication modules in bacterial signaling proteins.
    Annu Rev Genet. 1992;26:71-112 PMID: 1482126
  23. The short form of the CheA protein restores kinase activity and chemotactic ability to kinase-deficient mutants.
    Proc Natl Acad Sci U S A. 1993 Feb 15;90(4):1518-22 PMID: 8434013
  24. Signal transduction schemes of bacteria.
    Cell. 1993 Jun 4;73(5):857-71 PMID: 8098993
  25. Removal of the transducer protein from sensory rhodopsin I exposes sites of proton release and uptake during the receptor photocycle.
    Biophys J. 1993 Dec;65(6):2578-85 PMID: 8312493
  26. Two hypotheses--one answer. Sequence comparison does not support an evolutionary link between halobacterial retinal proteins including bacteriorhodopsin and eukaryotic G-protein-coupled receptors.
    FEBS Lett. 1994 Mar 28;342(1):7-11 PMID: 8143852
  27. A two-component system that regulates an osmosensing MAP kinase cascade in yeast.
    Nature. 1994 May 19;369(6477):242-5 PMID: 8183345
  28. Phototaxis of Halobacterium salinarium requires a signalling complex of sensory rhodopsin I and its methyl-accepting transducer HtrI.
    EMBO J. 1994 May 1;13(9):2150-5 PMID: 8187768
  29. Identification of volatile forms of methyl groups released by Halobacterium salinarium.
    J Biol Chem. 1994 Jun 10;269(23):16449-54 PMID: 8206953
  30. Effects of phosphorylation, Mg2+, and conformation of the chemotaxis protein CheY on its binding to the flagellar switch protein FliM.
    Biochemistry. 1994 Aug 30;33(34):10470-6 PMID: 8068685
  31. Signal transduction. Bringing the eukaryotes up to speed.
    Curr Biol. 1994 Mar 1;4(3):234-7 PMID: 7922328
  32. Sensory rhodopsin-controlled release of the switch factor fumarate in Halobacterium salinarium.
    Mol Microbiol. 1993 Dec;10(5):1077-85 PMID: 7934858
  33. Isolation of a prokaryotic photoreceptor: sensory rhodopsin from halobacteria.
    EMBO J. 1988 Sep;7(9):2925-33 PMID: 15977337
  34. Transformation methods for halophilic archaebacteria.
    Can J Microbiol. 1989 Jan;35(1):148-52 PMID: 2497937
  35. Methyl-accepting taxis proteins in Halobacterium halobium.
    EMBO J. 1989 Feb;8(2):631-9 PMID: 2721495
  36. Multiple kinetic states for the flagellar motor switch.
    J Bacteriol. 1989 Nov;171(11):6279-87 PMID: 2681161
  37. Sensory rhodopsins I and II modulate a methylation/demethylation system in Halobacterium halobium phototaxis.
    Proc Natl Acad Sci U S A. 1989 Oct;86(20):7746-50 PMID: 2682623
  38. Primary structure of sensory rhodopsin I, a prokaryotic photoreceptor.
    EMBO J. 1989 Dec 20;8(13):3963-71 PMID: 2591367
  39. Signal transduction in Halobacterium depends on fumarate.
    EMBO J. 1990 Feb;9(2):355-62 PMID: 2303030
  40. Tandem translation starts in the cheA locus of Escherichia coli.
    J Bacteriol. 1991 Mar;173(6):2116-9 PMID: 2002011
  41. Structural features of methyl-accepting taxis proteins conserved between archaebacteria and eubacteria revealed by antigenic cross-reaction.
    J Bacteriol. 1991 Sep;173(18):5837-42 PMID: 1909323
  42. Bacillus subtilis CheN, a homolog of CheA, the central regulator of chemotaxis in Escherichia coli.
    J Bacteriol. 1991 Dec;173(23):7443-8 PMID: 1938941
  43. Fumarate or a fumarate metabolite restores switching ability to rotating flagella of bacterial envelopes.
    J Bacteriol. 1992 Jan;174(2):643-5 PMID: 1729255
  44. Rhodopsin and phototransduction: a model system for G protein-linked receptors.
    FASEB J. 1992 Mar;6(6):2323-31 PMID: 1544542
  45. cheA, cheB, and cheC genes of Escherichia coli and their role in chemotaxis.
    J Bacteriol. 1976 May;126(2):758-70 PMID: 770453
Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1995-02-15
Pages
667-73
Language
English
Region
England
NLM ID
8208664
PMCID
PMC398130
Subset
IM
Databases
GENBANK
X82645
External Links
PubMed source PMC Full Text View journal details
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