A receptor scaffold mediates stimulus–response coupling in bacterial chemotaxis

doi:10.1054/ceca.1999.0075

Cell Calcium

Volume 26, Issue 5, November 1999, Pages 157-164

https://doi.org/10.1054/ceca.1999.0075 Get rights and content

Abstract

The mechanism of stimulus–response coupling in bacterial chemotaxis has emerged as a paradigm for understanding general features of intracellular signal transduction both in bacterial and eukaryotic cells. Until recently it was thought that the mechanism involved reversible stochastic interactions between dimeric receptors freely diffusing in the cytoplasmic membrane and several soluble signal transduction proteins within the cytoplasm. Recent results have shown that this view is an oversimplification. The receptors and most of the signal transduction proteins are organized together in a higher ordered structure at one pole of the bacterial cell. The scaffolding network within this structure appears to be composed of C-terminal α-helical extensions of the membrane chemoreceptor proteins held together in a lattice by tandem SH3-like domains. Results suggest that stimuli are detected through the perturbations they induce in scaffolding architecture.

References (68)

S. Djordjevic et al.
Structural analysis of bacterial chemotaxis proteins: components of a dynamic signaling system
J Struct Biol
(1998)
L. Turner et al.
Temperature dependence of switching of the bacterial flagellar motor by the protein CheY(13DK106YW)
Biophys J
(1999)
A.M. Bilwes et al.
Structure of CheA, a signal-transducing histidine kinase
Cell
(1999)
S.L. Mowbray et al.
Chemotaxis receptors: a progress report on structure and function
J Struct Biol
(1998)
W.G. Scott et al.
Refined structures of the ligand-binding domain of the aspartate receptor from Salmonella typhimurium
J Mol Biol
(1993)
S.L. Mowbray
Ribose and glucose-galactose receptors. Competitors in bacterial chemotaxis
J Mol Biol
(1992)
H. Le Moual et al.
Molecular evolution of the C-terminal cytoplasmic domain of bacterial receptors involved in taxis
J Mol Biol
(1996)
M. Surette et al.
Role of α-helical coiled-coil interactions in receptor dimerization, signaling, and adaptation during bacterial chemotaxis
J Biol Chem
(1996)
M. Surette et al.
Dimerization is required for the activity of the protein histidine kinase CheA that mediates signal transduction in bacterial chemotaxis
J Biol Chem
(1996)
T.W. Grebe et al.
The histidine protein kinase superfamily
Adv Microbial Physiol
(1999)

M. Kato et al.

Insights into multistep phosphorelay from the crystal structure of the C-terminal HPt domain of ArcB

Cell

(1997)

M. Levit et al.

Active site interference and asymmetric activation in the chemotaxis protein histidine kinase CheA

J Biol Chem

(1996)

S.S. Da Re et al.

Kinetics of CheY phosphorylation by small molecule phosphodonors

FEBS Lett

(1999)

J.A. Gegner et al.

Assembly of an MCP receptor, CheW, and kinase CheA complex in the bacterial chemotaxis signal transduction pathway

Cell

(1992)

K.A. Borkovich et al.

The dynamics of protein phosphorylation in bacterial chemotaxis

Cell

(1990)

J.B. Stock et al.

Signal transduction in bacterial chemotaxis

J Biol Chem

(1992)

D.L. Milligan et al.

Site-directed cross-linking. Establishment of the dimeric structure of the aspartate receptor of bacterial chemotaxis

J Biol Chem

(1988)

S. Clarke et al.

Membrane receptors for aspartate and serine in bacterial chemotaxis

J Biol Chem

(1979)

D.L. Milligan et al.

Purification and characterization of the periplasmic domain of the aspartate receptor

J Biol Chem

(1993)

W.G. Scott et al.

Refined structures of the ligand-binding domain of the aspartate receptor from Salmonella typhimurium

J Mol Biol

(1993)

A.H. West et al.

Crystal structure of the catalytic domain of the chemotaxis receptor methylesterase, CheB

J Mol Biol

(1995)

S. Djordjevic et al.

Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S-adenosylmethionine

Structure

(1997)

E.G. Ninfa et al.

Reconstitution of the bacterial chemotaxis signal transduction system from purified components

J Biol Chem

(1991)

S.L. Mowbray et al.

Additive independent responses in a single receptor: aspartate and maltose stimuli on the tar protein

Cell

(1987)

P. Dunten et al.

Tuning the responsiveness of a sensory receptor via covalent modification

J Biol Chem

(1991)

R.M. Macnab

Flagella and Motility

H.C. Berg et al.

Chemotaxis in Escherichia coli analysed by three-dimensional tracking

Nature

(1972)

J.B. Stock et al.

Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology

(1996)

M. Eisenbach

Control of bacterial chemotaxis

Mol Microbiol

(1996)

M.D. Manson et al.

Bacterial locomotion and signal transduction

J Bacteriol

(1998)

U. Alon et al.

Response regulator output in bacterial chemotaxis

Embo J

(1998)

B.E. Scharf et al.

Control of direction of flagellar rotation in bacterial chemotaxis

Proc Natl Acad Sci USA

(1998)

M.N. Levit et al.

Mechanism of CheA protein kinase activation in receptor signaling complexes

Biochemistry

(1999)

Cited by (0)

View full text

Invited reviewA receptor scaffold mediates stimulus–response coupling in bacterial chemotaxis

Abstract

J Struct Biol

Biophys J

Cell

J Struct Biol

J Mol Biol

J Mol Biol

J Mol Biol

J Biol Chem

J Biol Chem

Adv Microbial Physiol

Cell

J Biol Chem

FEBS Lett

Cell

Cell

J Biol Chem

J Biol Chem

J Biol Chem

J Biol Chem

J Mol Biol

J Mol Biol

Structure

J Biol Chem

Cell

J Biol Chem

Flagella and Motility

Chemotaxis in Escherichia coli analysed by three-dimensional tracking

Nature

Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology

Control of bacterial chemotaxis

Mol Microbiol

Bacterial locomotion and signal transduction

J Bacteriol

Response regulator output in bacterial chemotaxis

Embo J

Control of direction of flagellar rotation in bacterial chemotaxis

Proc Natl Acad Sci USA

Mechanism of CheA protein kinase activation in receptor signaling complexes

Biochemistry

Invited review
A receptor scaffold mediates stimulus–response coupling in bacterial chemotaxis