Regulation of PutA - Membrane associations by flavin adenine dinucleotide reduction

Biochemistry

Volumn 43, Issue 41, 2004, Pages 13165-13174

  Zhang, Weimin ^a   Zhou, Yuzhen ^a   Becker, Donald F ^a  

^a UNIVERSITY OF NEBRASKA LINCOLN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; CATALYSIS; CYTOLOGY; ENZYMES; ESCHERICHIA COLI; GENES; HYDROPHOBICITY; PHOTODISSOCIATION; PHOTOOXIDATION; PROTEINS;

DNA-BINDING ACTIVITY; KINETIC PARAMETERS; MEMBRANE ASSOCIATIONS; MEMBRANE BINDING;

NUCLEIC ACIDS;

BACTERIAL PROTEIN; FLAVINE ADENINE NUCLEOTIDE; FLAVOPROTEIN; GLUTAMIC ACID; PROLINE; PROLINE UTILIZATION A; SODIUM DITHIONITE; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CATALYSIS; CELLULAR DISTRIBUTION; COMPLEX FORMATION; CONTROLLED STUDY; DNA BINDING; ENZYME ACTIVITY; ESCHERICHIA COLI; GENE REPRESSION; GENETIC TRANSCRIPTION; LIPID BILAYER; LIPID VESICLE; MEMBRANE BINDING; MOLECULAR BIOLOGY; MOLECULAR INTERACTION; NONHUMAN; OXIDATION KINETICS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN LOCALIZATION; REDUCTION KINETICS; REGULATORY MECHANISM;

BACTERIAL PROTEINS; DNA-BINDING PROTEINS; ELECTROSTATICS; ESCHERICHIA COLI PROTEINS; FLAVIN-ADENINE DINUCLEOTIDE; INTRACELLULAR FLUID; LIGANDS; LIPID BILAYERS; MEMBRANE PROTEINS; OXIDATION-REDUCTION; PROLINE; PROLINE OXIDASE; PROTEIN BINDING; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 5444257841     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi048596g     Document Type: Article

References (48)

1. Wood, J. M. (1981) Genetics of L-proline utilization in Eschericia coli, J. Bacteriol. 146, 895-901.
2. Brown, E., and Wood, J. M. (1992) Redesigned purification yields a fully functional PutA protein dimer from Escherichia coli, J. Biol. Chem. 267, 13086-13092.
3. Abrahamson, J. L. A., Baker, L. G., Stephenson, J. T., and Wood, J. M. (1983) Proline dehydrogenase from Escherichia K12, properties of the membrane-associated enzyme, Eur. J. Biochem. 134, 77-82.
4. Graham, S., Stephenson, J. T., and Wood, J. M. (1984) Proline dehydrogenase from Escherichia coli K12, reconstitution of functional membrane association, J. Biol. Chem. 259, 2656-2661.
5. Ling, M., Allen, S. W., and Wood, J. M. (1994) Sequence analysis identifies the proline dehydrogenase and pyrroline-5-carboxylate dehydrogenase domains of the multifunctional Escherichia coli PutA protein, J. Mol. Biol. 245, 950-956.
6. +)-proline cotransport in Escherichia coli, J. Membr. Biol. 84, 157-164.
7. Chen, C. C., and Wilson, T. H. (1986) Solubilization and functional reconstitution of the proline transport system of Escherichia coli, J. Biol. Chem. 261, 2599-2604.
8. Nakao, T., Yamato, I., and Anraku, Y. (1987) Nucleotide sequence of putC, the regulatory region for the put regulon of Escherichia coli K12, Mol. Gen. Genet. 210, 364-368.
9. Scarpulla, R. C., and Soffer, R. L. (1978) Membrane-bound proline dehydrogenase from Escherichia coli, J. Biol. Chem. 253, 5997-6001.
10. Wood, J. (1987) Membrane association of proline dehydrogenase in Escherichia coli is redox dependent, Proc. Natl. Acad. Sci. U.S.A. 84, 373-377.
11. Menzel, R., and Roth, J. (1981) Enzymatic properties of the purified putA protein from Salmonella typhimurium, J. Biol. Chem. 256, 9762-9766.
12. Vinod, M. P., Bellur, P., and Becker, D. F. (2002) Electrochemical and functional characterization of the proline dehydrogenase domain of the PutA flavoprotein from Escherichia coli, Biochemistry 41, 6525-6532.
13. Lee, Y. H., Nadaraia, S., Gu, D., Becker, D. F., and Tanner, J. J. (2003) Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein, Nat. Struct. Biol. 10, 109-114.
14. Gu, D., Zhou, Y., Kallhoff, V., Baban, B., Tanner, J. J., and Becker, D. F. (2004) Identification and characterization of the DNA-binding domain of the multifunctional PutA flavoenzyme, J. Biol. Chem. 279, 31171-31176.
15. Surber, M. W., and Maloy, S. (1999) Regulation of flavin dehydrogenase compartmentalization: Requirements for PutA-membrane association in Salmonella typhimurium, Biochim. Biophys. Acta 1421, 5-18.
16. Brown, E. D., and Wood, J. M. (1993) Conformational change and membrane association of the PutA protein are coincident with reduction of its FAD cofactor by proline, J. Biol. Chem. 268, 8972-8979.
17. Muro-Pastor, A. M., Ostrovsky, P., and Maloy, S. (1997) Regulation of gene expression by repressor localization: Biochemical evidence that membrane and DNA binding by the PutA protein are mutually exclusive, J. Bacteriol. 179, 2788-2791.
18. Ostrovsky De Spicer, P., O'Brian, K., and Maloy, S. (1991) Regulation of proline utilization in Salmonella typhimurium: a membrane-associated dehydrogenase binds DNA in vitro, J. Bacteriol. 173, 211-219.
19. Zhu, W., and Becker, D. F. (2003) Flavin redox state triggers conformational changes in the PutA protein from Escherichia coli, Biochemistry 42, 5469-5477.
20. Becker, D. F., and Thomas, E. A. (2001) Redox properties of the PutA protein from Escherichia coli and the influence of the flavin redox state on PutA-DNA interactions, Biochemistry 40, 4714-4722.
21. Ostrovsky De Spicer, P., and Maloy, S. (1993) PutA protein, a membrane-associated flavin dehydrogenase, acts as a redox-dependent transcriptional regulator, Proc. Natl. Acad. Sci. U.S.A. 90, 4295-4298.
22. Muro-Pastor, A. M., and Maloy, S. (1995) Proline dehydrogenase activity of the transcriptional repressor PutA is required for induction of the put operon by proline, J. Biol. Chem. 270, 9819-9827.
23. Stahelin, R. V., and Cho, W. (2001) Differential roles of ionic, aliphatic, and aromatic residues in membrane-protein interactions: A surface plasmon resonance study on phospholipase A2, Biochemistry 40, 4672-4678.
24. Bitto, E., Li, M., Tikhonov, A. M., Schlossman, M. L., and Cho, W. (2000) Mechanism of annexin I-mediated membrane aggregation, Biochemistry 39, 13469-13477.
25. Papo, N., and Shai, Y. (2003) Exploring peptide membrane interaction using surface plasmon resonance: Differentiation between pore formation versus membrane disruption by lytic peptides, Biochemistry 42, 458-466.
26. Papo, N., and Shai, Y. (2004) Effect of drastic sequence alteration and D-amino acid incorporation on the membrane binding behavior of lytic peptides, Biochemistry 43, 6393-6403.
27. Mezel, V. A., and Knox, W. E. (1976) Properties and analysis of a stable derivative of pyrroline-5-carboxylic acid for use in metabolic studies, Anal. Biochem. 74, 430-440.
28. Strecker, H. J. (1957) The interconversion of glutamic acid and proline, J. Biol. Chem. 225, 825-834.
29. Hope, M. J., Bally, M. B., Webb, G., and Cullis, P. R. (1985) Production of large unilamellar vesicles by a rapid extrusion procedure. Characterization of size distribution, trapped volume and ability to maintain membrane potential, Biochim. Biophys. Acta 812, 55-65.
30. MacDonald, R. C., Ashley, G. W., Shida, M. M., Rakhmanova, V. A., Tarahovsky, Y. S., Pantazatos, D. P., Kennedy, M. T., Pozharski, E. V., Baker, K. A., Jones, R. D., Rosenzweig, H. S., Choi, K. L., Qiu, R., and McIntosh, T. J. (1999) Physical and biological properties of cationic triesters of phosphotidylcholine, Biophys. J. 77, 2612-2629.
31. Lewis, R. N. A., Prenner, E. J., Kondejewski, L. H., Flach, C. R., Mednelsohn, R., Hodges, R. S., and McElhaney, R. N. (1999) Fourier transform infrared spectroscopic studies of the interaction of the antimicrobial peptide gramicidin S with lipid micelles and with lipid monolayer and bilayer membranes, Biochemistry 38, 15193-15203.
32. Erb, E. M., Chen, X., Allen, S., Roberts, C. J., Tendler, S. J. B., Davies, M. C., and Forsen, S. (2000) Characterization of the surfaces generated by liposome binding to the modified dextran matrix of a surface plasmon resonance sensor chip, Anal. Biochem. 280, 29-35.
33. Myszka, D. G. (1997) Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors, Curr. Opin. Biotechnol. 8, 50-57.
34. Zhu, W., Gincherman, Y., Docherty, P., Spilling, C. D., and Becker, D. F. (2002) Effects of proline analog binding on the spectroscopic and redox properties of PutA, Arch. Biochem. Biophys. 408, 131-136.
35. Bittova, L., Sumandea, M., and Cho, W. (1999) A structure-function study of the C2 domain of cytosolic phospholipase A2, J. Biol. Chem. 274, 9665-9672.
36. Ermakov, Y. A., Averbakh, A. Z., Yusipovich, A. I., and Sukharev, S. (2001) Dipole potentials indicate restructuring of the membrane interface induced by gadolinium and beryllium ions, Biophys. J. 80, 1851-1862.
37. +/proline transporter of Escherichia coli, Biochemistry 37, 11083-11088.
38. +/proline transporter of Escherichia coli, J. Biol. Chem. 273, 26400-26407.
39. +/proline transporter PutP of Escherichia coli forms part of a conformationally flexible, cytoplasmic exposed aqueous cavity within the membrane, J. Biol. Chem. 278, 42942-42949.
40. Koland, J. G., Miller, M. J., and Gennis, R. B. (1984) Reconstitution of the membrane-bound, ubiquinone-dependent pyruvate oxidase respiratory chain of Escherichia coli with the cytochrome d terminal oxidase, Biochemistry 23, 445-453.
41. Russell, P., Hager, L. P., and Gennis, R. B. (1977) Characterization of the proteolytic activation of pyruvate oxidase, J. Biol. Chem. 252, 7877-7882.
42. Schrock, H. L., and Gennis, R. B. (1977) High affinity lipid binding sites on the peripheral membrane enzyme pyruvate oxidase, J. Biol. Chem. 252, 5990-5995.
43. Schrock, H. L., and Gennis, R. B. (1980) The binding of a fluorescent activator 2-(N-decyl)aminonaphthalene-6-sulfonic acid to pyruvate oxidase, Biochim. Biophys. Acta 615, 10-18.
44. Chang, Y.-Y., and Cronan, J. E. J. (1995) Detection by site-specific disulfide cross-linking of a conformational change in binding of Escherichia coli pyruvate oxidase to lipid bilayers, J. Biol. Chem. 270, 7896-7901.
45. Chang, Y.-Y., and Cronan, J. E. J. (1997) Sulfhydryl chemistry detects three conformations of the lipid binding region of Escherichia coli pyruvate oxidase, Biochemistry 36, 11564-11573.
46. Recny, M. A., and Hager, L. P. (1983) Isolation and characterization of the protease-activated form of pyruvate oxidase. Evidence for a conformational change in the environment of the flavin prosthetic group, J. Biol. Chem. 258, 5189-519.
47. Russell, P., Schrock, H. L., and Gennis, R. B. (1977) Lipid activation and protease activation of pyruvate oxidase, J. Biol. Chem. 252, 7883-7887.
48. Zhang, M., White, T. A., Schuerman, J. P., Baban, B. A., Becker, D. F., and Tanner, J. J. (2004) Structures of the Escherichia coli PutA Proline Dehydrogenase Domain in Complex with Competitive Inhibitors, Biochemistry, in press.