Abstract

Bacterial chemotaxis is one of a large number of sensory systems in bacteria that use two proteins, a histidine dependent protein kinase and the response regulator protein that is the kinase substrate. We propose to use modern nuclear magnetic resonance techniques to study the structures, dynamics and structural consequences of phosphorylation of three response regulators. These include: CheY, a member of the chemotaxis sensory transduction pathway in Escherichia coli; and SpoOF and SpoOA, members of the sporulation sensory transduction pathway in Bacillus subtilis. These three response regulators appear the have related distinct functions associated with the phosphorylation event and we hope to define the structural bases of these functional differences. We will also examine the structure of domains of the kinase CheA and the complex formed between CheA and CheY.
The aim of this part of the proposal is to define the nature of the specific recognition between the kinase and its cognate response regulator(s).

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM059544-22
Application #
6520047
Study Section
Molecular and Cellular Biophysics Study Section (BBCA)
Program Officer
Li, Jerry
Project Start
1981-04-01
Project End
2003-06-30
Budget Start
2002-06-01
Budget End
2003-06-30
Support Year
22
Fiscal Year
2002
Total Cost
$244,580
Indirect Cost

  Institution

Name
University of Oregon
Department
Biochemistry
Type
Organized Research Units
DUNS #
948117312
City
Eugene
State
OR
Country
United States
Zip Code
97403

  Publications

Ding, Xueye; He, Qiang; Shen, Fenglin et al. (2018) Regulatory Role of an Interdomain Linker in the Bacterial Chemotaxis Histidine Kinase CheA. J Bacteriol 200:
Dahlquist, Frederick W (2018) The Bacterial Flagellar Motor Continues to Amaze. Biophys J 114:505-506
Barnes, Ryan; Sun, Sheng; Fichou, Yann et al. (2017) Spatially Heterogeneous Surface Water Diffusivity around Structured Protein Surfaces at Equilibrium. J Am Chem Soc 139:17890-17901
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
Lynch, Michael J; Levenson, Robert; Kim, Eun A et al. (2017) Co-Folding of a FliF-FliG Split Domain Forms the Basis of the MS:C Ring Interface within the Bacterial Flagellar Motor. Structure 25:317-328
Kang, Di; Sun, Sheng; Kurnik, Martin et al. (2017) New Architecture for Reagentless, Protein-Based Electrochemical Biosensors. J Am Chem Soc 139:12113-12116
Pan, Wenlin; Dahlquist, Frederick W; Hazelbauer, Gerald L (2017) Signaling complexes control the chemotaxis kinase by altering its apparent rate constant of autophosphorylation. Protein Sci 26:1535-1546
Wang, Xiqing; Vallurupalli, Pramodh; Vu, Anh et al. (2014) The linker between the dimerization and catalytic domains of the CheA histidine kinase propagates changes in structure and dynamics that are important for enzymatic activity. Biochemistry 53:855-61
Ortega, Davi R; Mo, Guoya; Lee, Kwangwoon et al. (2013) Conformational coupling between receptor and kinase binding sites through a conserved salt bridge in a signaling complex scaffold protein. PLoS Comput Biol 9:e1003337
Wang, Xiqing; Wu, Chun; Vu, Anh et al. (2012) Computational and experimental analyses reveal the essential roles of interdomain linkers in the biological function of chemotaxis histidine kinase CheA. J Am Chem Soc 134:16107-10

Showing the most recent 10 out of 25 publications