The study of bacterial chemotaxis offers an approach to understanding the basic fundamentals of the biological signalling systems at the ultimate molecular level. As more is learned about sensory-signalling systems of higher eucaryotes such as the visual system or the hormone receptor systems, it has become obvious that bacterial chemotaxis is not a model for these phenomena but rather another example of the same basic biochemical mechanism. Because of the similarity of all of the signalling systems, understanding of an aspect of one system has immediately been applicable to the others. For example, the GTPase activity of the transducin protein of the visual system is now known to be analogous to the GTPase activity of the G protein in the beta-adrenergic hormone system. Covalent modification of the signaller by methylation in bacteria is analogous to phosphorylation of the signaller in the rhodopsin system. One of the advantages of the bacterial system is the wealth of genetic data accumulated over the years. There are greater than 40 genes and 12 operons required for a fully functioning chemotaxis system in E.coli. It is this availability of genetics which allows the bacterial system to gain insight not possible with the eucaryotic systems. For example, the genetics has been used to identify all of the gene products involved in bacterial sensory reception and signal transduction. Therefore, all of the parts of the system are known. On the other hand, some aspects of biochemical analysis are more advanced in the higher eucaryotic systems. This has been true because sensory organs, such as bovine eyes, are readily available in large quantity. It has not, however, been possible in the past to isolate the sensory organelle from bacteria. Now, by exploiting in vitro genetic recombination, it has been possible to overproduce and purify milligram quantities of individual chemotaxis proteins. this ability coupled with the well-developed genetics and the biochemical precedents developed in higher systems will enable the sensory system of bacertial chemotaxis to be understood at the molecular level.

Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Research Project (R01)
Project #
5R01AI018985-06
Application #
3128385
Study Section
Microbial Physiology and Genetics Subcommittee 2 (MBC)
Project Start
1982-04-01
Project End
1990-03-31
Budget Start
1987-04-01
Budget End
1988-03-31
Support Year
6
Fiscal Year
1987
Total Cost
Indirect Cost
Name
University of Illinois at Chicago
Department
Type
Schools of Arts and Sciences
DUNS #
121911077
City
Chicago
State
IL
Country
United States
Zip Code
60612
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Shukla, D; Zhu, X Y; Matsumura, P (1998) Flagellar motor-switch binding face of CheY and the biochemical basis of suppression by CheY mutants that compensate for motor-switch defects in Escherichia coli. J Biol Chem 273:23993-9
Pruss, B M (1998) Acetyl phosphate and the phosphorylation of OmpR are involved in the regulation of the cell division rate in Escherichia coli. Arch Microbiol 170:141-6
Halkides, C J; Zhu, X; Phillion, D P et al. (1998) Synthesis and biochemical characterization of an analogue of CheY-phosphate, a signal transduction protein in bacterial chemotaxis. Biochemistry 37:13674-80
Dowd, J P; Matsumura, P (1997) The use of flash photolysis for a high-resolution temporal and spatial analysis of bacterial chemotactic behaviour: CheZ is not always necessary for chemotaxis. Mol Microbiol 25:295-302
Pruss, B M; Matsumura, P (1997) Cell cycle regulation of flagellar genes. J Bacteriol 179:5602-4
Zhu, X; Rebello, J; Matsumura, P et al. (1997) Crystal structures of CheY mutants Y106W and T87I/Y106W. CheY activation correlates with movement of residue 106. J Biol Chem 272:5000-6
Wang, H; Matsumura, P (1997) Phosphorylating and dephosphorylating protein complexes in bacterial chemotaxis. J Bacteriol 179:287-9
Zhu, X; Volz, K; Matsumura, P (1997) The CheZ-binding surface of CheY overlaps the CheA- and FliM-binding surfaces. J Biol Chem 272:23758-64
Amsler, C D (1996) Use of computer-assisted motion analysis for quantitative measurements of swimming behavior in peritrichously flagellated bacteria. Anal Biochem 235:20-5

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