Michael D. Manson

Thanks, Charley.

A NarX-Tar chimera mediates repellent chemotaxis to nitrate and nitrite.

CheZ phosphatase localizes to chemoreceptor patches via CheA-short.

A sensitive, versatile microfluidic assay for bacterial chemotaxis.

Rusty, jammed, and well-oiled hinges: Mutations affecting the interdomain region of FliG, a rotor element of the Escherichia coli flagellar motor.

Tryptophan residues flanking the second transmembrane helix (TM2) set the signaling state of the Tar chemoreceptor.

Cooperative signaling among bacterial chemoreceptors.

Mutationally altered signal output in the Nart (NarX-Tar) hybrid chemoreceptor.

The Escherichia coli MotAB proton channel unplugged.

How 34 pegs fit into 26 + 8 holes in the flagellar motor.

Tuning a bacterial chemoreceptor with protein-membrane interactions.

Clusters of charged residues at the C terminus of MotA and N terminus of MotB are important for function of the Escherichia coli flagellar motor.

The tie that binds the dynamic duo: the connector between AS1 and AS2 in the HAMP domain of the Escherichia coli Tsr chemoreceptor.

The region preceding the C-terminal NWETF pentapeptide modulates baseline activity and aspartate inhibition of Escherichia coli Tar.

Flow-based microfluidic device for quantifying bacterial chemotaxis in stable, competing gradients.

Protein domains and residues involved in the CheZ/CheAS interaction.

A grand view of the flagellar motor.

A mutational wrench in the HAMP gearbox.

Microfluidic techniques for the analysis of bacterial chemotaxis.

Repellent taxis in response to nickel ion requires neither Ni2+ transport nor the periplasmic NikA binding protein.

Investigation of bacterial chemotaxis in flow-based microfluidic devices.

Dynamic motors for bacterial flagella.

Mutational analysis of the transmembrane helix 2-HAMP domain connection in the Escherichia coli aspartate chemoreceptor tar.

Chemotaxis to the quorum-sensing signal AI-2 requires the Tsr chemoreceptor and the periplasmic LsrB AI-2-binding protein.

Not too loose, not too tight--just right. Biphasic control of the Tsr HAMP domain.

Transmembrane signaling is anything but rigid.