- Michael Manson
- Professor of Biology, and of Biochemistry and Biophysics
- BSBE / Room 301A
- Undergraduate Education
- B.A. Johns Hopkins University (1969)
- Graduate Education
- Ph.D. Stanford University (1975)
- Postdoc. University of Colorado, Boulder (1975-79)
- California Institute of Technology (1980-81)
- Joined Texas A&M in 1987
Bacterial Chemotaxis, Motility & Their Use in Biotechnology
The most obvious behavior of Escherichia coli is chemotaxis. Bacteria swim in a 3-D random walk of alternating “runs” and “tumbles.” Cells extend runs towards chemicals they like (attractants) and away from chemicals they do not (repellents). Swimming is propelled by rotation of rigid helical filaments that are driven at their bases by motors powered by a transmembrane proton current. Counterclockwise rotation causes runs, clockwise rotation causes tumbles. We investigate how this tiny (<50 nm diameter) motor assembles from its component proteins and how the proton current couples to rotation. We also study how transmembrane chemoreceptors bind attractants or interact with periplasmic proteins that bind them, how the signal is propagated across the membrane (transmembrane signaling is a function of all cell-surface receptors), and how these signals are integrated and amplified within the cell.
Nanotechnology is a new focus of our group. Starting with chemoreceptors and the functionally related family of transmembrane sensor kinases, we are engineering bacteria to be versatile, efficient, and low-cost detectors of chemicals in the environment. We are also working with mechanical engineers to turn bacteria into miniature beasts of burden to deliver tiny cargo to specified destinations and to harness flagellar motors as system-internal pumps to generate flow in microchannels.
Sule, N, Pasupuleti, S, Kohli, N, Menon, R, Dangott, LJ, Manson, MD et al.. The Norepinephrine Metabolite 3,4-Dihydroxymandelic Acid Is Produced by the Commensal Microbiota and Promotes Chemotaxis and Virulence Gene Expression in Enterohemorrhagic Escherichia coli. Infect. Immun. 2017; :.
Pasupuleti, S, Sule, N, Cohn, WB, MacKenzie, DS, Jayaraman, A, Manson, MD et al.. Chemotaxis of Escherichia coli to norepinephrine (NE) requires conversion of NE to 3,4-dihydroxymandelic acid. J. Bacteriol. 2014;196 (23):3992-4000.
Zhao, X, Zhang, K, Boquoi, T, Hu, B, Motaleb, MA, Miller, KA et al.. Cryoelectron tomography reveals the sequential assembly of bacterial flagella in Borrelia burgdorferi. Proc. Natl. Acad. Sci. U.S.A. 2013;110 (35):14390-5.
Adase, CA, Draheim, RR, Rueda, G, Desai, R, Manson, MD. Residues at the cytoplasmic end of transmembrane helix 2 determine the signal output of the TarEc chemoreceptor. Biochemistry. 2013;52 (16):2729-38.
Liu, J, Hu, B, Morado, DR, Jani, S, Manson, MD, Margolin, W et al.. Molecular architecture of chemoreceptor arrays revealed by cryoelectron tomography of Escherichia coli minicells. Proc. Natl. Acad. Sci. U.S.A. 2012;109 (23):E1481-8.
Adase, CA, Draheim, RR, Manson, MD. The residue composition of the aromatic anchor of the second transmembrane helix determines the signaling properties of the aspartate/maltose chemoreceptor Tar of Escherichia coli. Biochemistry. 2012;51 (9):1925-32.
Manson, MD. Transmembrane signaling is anything but rigid. J. Bacteriol. 2011;193 (19):5059-61.
Manson, MD. Not too loose, not too tight--just right. Biphasic control of the Tsr HAMP domain. Mol. Microbiol. 2011;80 (3):573-6.
Hegde, M, Englert, DL, Schrock, S, Cohn, WB, Vogt, C, Wood, TK et al.. Chemotaxis to the quorum-sensing signal AI-2 requires the Tsr chemoreceptor and the periplasmic LsrB AI-2-binding protein. J. Bacteriol. 2011;193 (3):768-73.
Wright, GA, Crowder, RL, Draheim, RR, Manson, MD. Mutational analysis of the transmembrane helix 2-HAMP domain connection in the Escherichia coli aspartate chemoreceptor tar. J. Bacteriol. 2011;193 (1):82-90.