On Going Research Support:
5 R01 GM 059484-04 Matsumura (PI) 05/01/99- 04/30/03
NIH/NIGMS
Combinatorial Complex-Driven Global Regulation of Transcription
The major goals of this project are to study how the FlhD/C heterotetramer regulates the flagellar regulon and how FlhD without FlhC regulates other operons.
Role: PI

5 R01GM 062044-20 Matsumura (PI) 04/1/82-06/30/04
NIH/NIGMS
Molecular Biology of the Mot and Che Gene Products
The major goals of this project are to study the structure and function of CheY, by solving the solution NMR structure of the phosphorylated form of CheY and to define the molecular mechanism of activation.
Role: PI

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Selected Publications:

1. McNally, D.F. and P. Matsumura. (1991) Chemotaxis signalling complexes: physical association of CheW with CheA alters autophosphorylation rates of CheA in response to the signalling state of the receptors and increases CheA binding to CheY. Proc. Nat. Acad. Sci., USA. 88: 6269-6273.
2. Volz, K. and P. Matsumura. (1991) Crystal structure of Escherichia coli CheY refined at 1.7 Å resolution. J. Bio. Chem. 266: 15511-15519.
3. Roman, S.J., M. Myers, K. Volz and P. Matsumura. (1992) A Chemotactic signalling surface on CheY defined by suppressors of flagellar switch mutations. J. Bacteriol. 174: 6247-6255.
4. Kar. L., P. Matsumura and M. E. Johnson. (1992) Bivalent-metal binding to CheY protein. Biochem. J. 287: 521-531
5. Kar, L., P. Z. De Croos, S.J. Roman, P. Matsumura and M. E. Johnson. (1992) Specificity and affinity of binding of phosphate-containing compounds to CheY protein. Biochem. J. 287: 533-543.
6. Amsler, C. D., M. Cho and P. Matsumura (1993) Multiple factors underlying the maximum motility of Escherichia coli as cultures enter post-exponential growth. J. Bacteriology 175: 6247-6255.
7. Roman, S. J., B. B. Frantz and P. Matsumura. (1993) Gene sequence, overproduction, purification and determination of the wild-type level of the Escherichia coli flagellar switch protein FliG. Gene. 133: 103-108.
8. Lowry, D. F., A. Roth, P. Rupert, F.W. Dahlquist, F. Moy, P. Domaile and P. Matsumura. (1994) Signal Transduction in Chemotaxis; a propagating conformation change upon phosphorylation of CheY. Biochem. J. 269: 26358-26362.
9. Moy, J.F., D.F. Lowry, P. Matsumura, F.W. Dahlquist, J.E. Krywko and P.J. Domaille. (1994) Assignments, secondary structure, global fold and dynamics of CheY using three- and four-dimensional heteronuclear (13C, 15N) NMR spectroscopy. Biochemistry. 33: 10731-10742.
10. Amsler, C. D. and P. Matsumura. (1994) Chemotactic Signal Transduction in Escherichia coli and Salmonella typhimurium. In Signal Transducing Genetic Switches. Eds. J.A. Hoch and T. Silhavy.pp 89- 103.
11. Ganguli, S., H. Wang, P. Matsumura and K. Volz. (1995) Uncoupled phosphorylation and activation in bacterial chemotaxis. the 2.1 D structure of threonine to isoleucine mutant at position 87 of CheY. J. Biol. Chem. 270: 17386-17393.
12. Shukla, D. and P. Matsumura. (1995) Mutations leading to altered CheA binding cluster on a face of CheY. J. Biol. Chem. 270: 24414-24419.
13. Wang, H. and P. Matsumura. (1995) Characterization of the CheAs/CheZ complex: a specific interaction resulting in enhanced dephosphorylating activity on CheY-P. Mol. Microbiol. 19: 695-703.
14. Swanson, R.V., D.F. Lowry, P. Matsumura, M.M. McEvoy, M.I. Simon, and F.W. Dahlquist. (1995) Localized perturbations in CheY structure monitored by NMR identify a CheA binding interface. Nat. Struct. Biol. 2: 906-910.
15. Zhao, R., C.D. Amsler, P. Matsumura, and S. Khan. (1996) FliG and FliM distribution in the Salmonella typhimurium cell and flagellar basal bodies. J. Bacteriol. 178: 258-265.
16. Wang, H and P. Matsumura(1996) Characterization of the CheAS/CheZ complex: a specific interaction resulting in enhanced dephosphorylation activity on CheY-phosphate. Mol. Microbiol. 19: 4,695-703.
17. Zhu, X., C.D. Amsler, K. Volz, and P. Matsumura. (1996) Behavioral and biochemical consequences of substitutions of tyrosine 106 of CheY: evidence for an important role in bacterial chemotaxis signal transduction. J. Bacteriol. 178: 14,4208-4215.
18. Wang, H and P. Matsumura. (1997) Phosphorylating and Dephosphorylating Complexes in Bacterial Chemotaxis. J. Bacteriol. 179: 1,287-289.
18. Zhu, X., J. Rebello, P. Matsumura and K. Volz. (1997) Crystal Structures of CheY Mutants Y106W and T87I/Y106W. J. Biol. Chem, 272: 8,5000-5006.
19. Dowd, J. and P. Matsumura. (1997) The Use of Flash Photolysis For a High-Resolution Temporal and Spatial Analysis of Bacterial Chemotactic Behavior: CheZ is not Always Required for Chemotaxis. Mol.
Microbiology ,25: 295-308.
20. Zhu,X., K. Volz, and P. Matsumura. (1997) The CheZ Binding and Catalytic Regions on CheY: The CheZ
Binding Surface of CheY Overlaps the CheA and FliM Binding Surface. Journal of Biol. Chem. 272: 23758- 23764.
21. Shukla, D., Zhu., X., and P. Matsumura. ( 1998) Flagellar Motor-Switch Binding Face of CheY and The Biochemical Basis of Suppression by CheY Mutants Which Compensate for Motor-Switch Defects in
Escherichia coli. Journal of Biol. ChemVol. 273: 23993-23999.
22. Halkides, C.J.., Zhu, X., Matsumura, P., and F. W. Dahlquist. (1998) Synthesis and biochemical characterization of an analog of CheY-phosphate, a signal transduction protein in bacterial chemotaxis Biochemistry; 37(39): 13674-80.
23. Halkides, C. J., M. M. McEvoy, E. Casper, P. Matsumura, K. Volz and F. W. Dahlquist. (2000) The 1.9 Resolution Structure of Phosphono-CheY, An Analogue of the Active Form of the Response Regulator, CheY. Biochemistry, 39: 5280-5286.