Regulation of flavin dehydrogenase compartmentalization: Requirements for PutA-membrane association in Salmonella typhimurium

Biochimica et Biophysica Acta - Biomembranes

Volumn 1421, Issue 1, 1999, Pages 5-18

  Surber, Mark W ^a   Maloy, Stanley ^a  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

Autogenous regulation; Compartmentalization; Peripheral membrane protein; Proline dehydrogenase; Proline utilization

Indexed keywords

CYTOCHROME B; LIPOSOME; MEMBRANE PROTEIN; OXIDOREDUCTASE; UBIQUINONE;

ARTICLE; ENZYME ACTIVITY; ENZYME BINDING; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTEIN TRANSPORT; SALMONELLA TYPHIMURIUM;

BACTERIAL PROTEINS; BINDING SITES; ELECTRON TRANSPORT; FLAVIN-ADENINE DINUCLEOTIDE; LIPOSOMES; MEMBRANE LIPIDS; MEMBRANE PROTEINS; OXIDATION-REDUCTION; PROLINE; PROLINE OXIDASE; QUINONES; SALMONELLA TYPHIMURIUM;

ESCHERICHIA COLI; SALMONELLA TYPHIMURIUM; TYPHIMURIUM;

EID: 0032852996     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2736(99)00104-2     Document Type: Article

References (38)

1. J. Cronan, R. Gennis, S. Maloy, The cytoplasmic membrane, in: F.C. Neidhardt, J.L. Ingraham, K.B. Low, B. Magasanik, M. Schaechter, H.E. Umbarger (Eds.), Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology, American Society for Microbiology, Washington, DC, 1987, pp. 31-55.
2. M.E. Varga, J.H. Weiner, Biochem. Cell. Biol. 73 (1995) 47-153.
3. L. Hederstedt, T. Ohnishi, Progress in succinate:quinone oxidoreductase research, in: L. Ernster (Ed.), Molecular Mechanisms in Bioenergetics, Elsevier Science, New York, 1992, pp. 163-198.
4. J. Koland, M. Mather, R. Gennis, J. White, L. Hager, Activation of pyruvate oxidase and interaction with membrane components, in: Martonosi (Ed.), Membrane Transport, Plenum Press, New York, 1982, pp. 83-92.
5. J. Kohland, M. Miller, R. Gennis, Biochemistry 23 (1984) 445-453.
6. A. Asano, T. Kaneshiro, A.F. Brodie, J. Biol. Chem. 240 (1965) 895-905.
7. A.H. Goldie, S. Narindrasorasak, B.D. Sanwal, Biochem. Biophys. Res. Commun. 83 (1978) 421-426.
8. S. Narindrasorasak, A.H. Goldie, B.D. Sanwal, J. Biol. Chem. 254 (1979) 1540-1545.
9. H.-F. Kung, U. Henning, Proc. Natl. Acad. Sci. USA 69 (1972) 925-929.
10. S. Maloy, The proline utilization operon, in: F.C. Neidhardt, J.L. Ingraham, K.B. Low, B. Magasanik, M. Schaechter, H.E. Umbarger (Eds.), Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology, American Society for Microbiology, Washington, DC, 1987, pp. 1513-1519.
11. P. Ostrovsky de Spicer, K. O'Brien, S. Maloy, J. Bacteriol. 173 (1991) 211-219.
12. E.D. Brown, J.M. Wood, J. Biol. Chem. 267 (1992) 13066-13092.
13. A. Muro-Pastor, P. Ostrovsky, S. Maloy, J. Bacteriol. 179 (1997) 2788-2791.
14. J.M. Wood, Proc. Natl. Acad. Sci. USA 84 (1987) 373-377.
15. R. Menzel, J. Roth, J. Biol. Chem. 256 (1981) 9755-9761.
16. J.L. Abrahamson, L.G. Baker, J.T. Stephenson, J.M. Wood, Eur. J. Biochem. 134 (1983) 77-82.
17. S.B. Graham, J.T. Stephenson, J.M. Wood, J. Biol. Chem. 259 (1984) 2656-2661.
18. M.W. Surber, S. Maloy, Arch. Biochem. Biophys. 354 (1998) 281-287.
19. R. Menzel, J. Roth, J. Biol. Chem. 256 (1981) 9762-9766.
20. P. Ostrovsky de Spicer, S. Maloy, Proc. Natl. Acad. Sci. USA 90 (1993) 4295-4298.
21. E.D. Brown, J.M. Wood, J. Biol. Chem. 268 (1993) 8972-8979.
22. A.M. Muro-Pastor, S. Maloy, J. Biol. Chem. 270 (1995) 9819-9827.
23. B.J. Wallace, I.G. Young, Biochim. Biophys. Acta 461 (1977) 84-100.
24. H. Vogel, D. Bonner, J. Biol. Chem. 218 (1956) 97-106.
25. G.F. Ames, J. Bacteriol. 95 (1968) 833-843.
26. I. Stern, B. Shapiro, J. Clin. Pathol. 6 (1953) 158.
27. R.C. MacDonald, R.I. MacDonald, B.Ph.M. Menco, K. Takeshita, N.K. Subbarao, L. Hu, Biochim. Biophys. Acta 1061 (1991) 297-303.
28. H.J. Strecker, J. Biol. Chem. 225 (1957) 825-834.
29. C. Bordier, J. Biol. Chem. 256 (1981) 1604-1607.
30. J.C. Pryde, Trends Biochem. Sci. 11 (1986) 160-163.
31. D. Berkowitz, J. Huston, H. Whitfield, J. Roth, B. Ames, J. Bacteriol. 96 (1968) 215-220.
32. H.L. Schrock, R.B. Gennis, Biochim. Biophys. Acta 614 (1980) 215-220.
33. C. Huang, J.T. Mason, Proc. Natl. Acad. Sci. USA 75 (1978) 308-310.
34. K. Ekena, S. Maloy, Mol. Gen. Genet. 220 (1990) 492-494.
35. J. Vervoort, F. Muller, S.G. Mayhew, W.A.M. van den Berg, C.T.W. Moonen, A. Bacher, Biochemistry 25 (1986) 6789-6799.
36. S. Pust, J. Vervoort, K. Decker, A. Bacher, F. Muller, Biochemistry 28 (1989) 516-521.
37. C. Sanner, P. Macheroux, H. Ruterjans, F. Muller, A. Bacher, Eur. J. Biochem. 196 (1991) 663-672.
38. P. Kierkegaard, R. Norrestam, P.-E. Werner, I. Csoregh, M. Von Glehn, R. Karlsson, M. Leijonmarck, O. Ronnquist, B. Stensland, O. Tillberg, L. Torbjornsson, in: H. Kamin (Ed.), Proceedings of the Third International Symposium on Flavins and Flavoproteins, University Park Press, Baltimore, MD, 1971, pp. 1-22.