Bacterial chemotaxis exhibits many of the properties of sensory systems in higher organisms, and is viewed as a useful model for studying the molecular basis of sensory transduction events. The longterm objective of this work is to understand the process of chemosensory transduction in Escherichia coli at the molecular level. The components of the signaling pathway responsible for chemotactic behavior in E. coli have been identified, but their functions are not yet understood.
The specific aim of this project is to explore structurefunction relationships in some of these transduction components: Tar and Tsr, inner membrane proteins that serve as chemoreceptors and signal transducers; CheA, CheW, CheY and CheZ, cytoplasmic proteins that play various roles in transmission of sensory signals between the transducers and the flagellar rotational machinery; and MotA and MotB, inner membrane proteins that are required for flagellar rotation. Plasmids carrying the structural genes for these proteins will be mutagenized in vitro and screened for various sorts of functional defects, including dominant mutations that may specifically affect interactions with other transduction components. Reversion analyses of these mutants will be done to identify the targets of the dominant effects, and to define proteinprotein interactions among the signaling elements. The DNA sequence changes in selected mutants will be determined in order to delineate functional domains within the proteins. From these studies, structurefunction models will be devised that can be tested by sitespecific mutagenesis.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
2R01GM019559-15
Application #
3269688
Study Section
Microbial Physiology and Genetics Subcommittee 2 (MBC)
Project Start
1979-06-01
Project End
1992-05-31
Budget Start
1987-06-01
Budget End
1988-05-31
Support Year
15
Fiscal Year
1987
Total Cost
Indirect Cost
Name
University of Utah
Department
Type
Schools of Arts and Sciences
DUNS #
City
Salt Lake City
State
UT
Country
United States
Zip Code
84112
Flack, Caralyn E; Parkinson, John S (2018) A zipped-helix cap potentiates HAMP domain control of chemoreceptor signaling. Proc Natl Acad Sci U S A 115:E3519-E3528
Piñas, Germán E; DeSantis, Michael D; Parkinson, John S (2018) Noncritical Signaling Role of a Kinase-Receptor Interaction Surface in the Escherichia coli Chemosensory Core Complex. J Mol Biol 430:1051-1064
Lai, Run-Zhi; Han, Xue-Sheng; Dahlquist, Frederick W et al. (2017) Paradoxical enhancement of chemoreceptor detection sensitivity by a sensory adaptation enzyme. Proc Natl Acad Sci U S A 114:E7583-E7591
Lai, Run-Zhi; Gosink, Khoosheh K; Parkinson, John S (2017) Signaling Consequences of Structural Lesions that Alter the Stability of Chemoreceptor Trimers of Dimers. J Mol Biol 429:823-835
Frank, Vered; Piñas, Germán E; Cohen, Harel et al. (2016) Networked Chemoreceptors Benefit Bacterial Chemotaxis Performance. MBio 7:
Ames, Peter; Hunter, Samuel; Parkinson, John S (2016) Evidence for a Helix-Clutch Mechanism of Transmembrane Signaling in a Bacterial Chemoreceptor. J Mol Biol 428:3776-88
Piñas, Germán E; Frank, Vered; Vaknin, Ady et al. (2016) The source of high signal cooperativity in bacterial chemosensory arrays. Proc Natl Acad Sci U S A 113:3335-40
Parkinson, John S; Hazelbauer, Gerald L; Falke, Joseph J (2015) Signaling and sensory adaptation in Escherichia coli chemoreceptors: 2015 update. Trends Microbiol 23:257-66
Mowery, Patricia; Ames, Peter; Reiser, Rebecca H et al. (2015) Chemotactic Signaling by Single-Chain Chemoreceptors. PLoS One 10:e0145267
Kitanovic, Smiljka; Ames, Peter; Parkinson, John S (2015) A Trigger Residue for Transmembrane Signaling in the Escherichia coli Serine Chemoreceptor. J Bacteriol 197:2568-79

Showing the most recent 10 out of 45 publications