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Site-Directed Mutagenesis of Rhodobacter sphaeroides Reaction Center: The Role of Tyrosine L222

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Current Research in Photosynthesis

Abstract

Reaction centers (RCs) from purple photosynthetic bacteria have been used as a model system for the study of herbicides which act as competitive inhibitors of the secondary quinone, QB, of the acceptor quinone complex (1). The x-ray structures of RCs for Rps. viridis (2) and Rb. sphaeroides (3) have revealed some details of the QB/herbicide binding domain, as well as features of the interaction. Many herbicide resistant mutants have been isolated by various groups by selecting cells that grow in the presence of herbicide (4,5). However, it is now possible to learn more about the structure/function relationships of the RC by selectively altering any amino acid in the QB binding domain through site-directed mutagenesis. Here, we report the construction of a RC deletion mutant of Rb. sphaeroides which can be complemented by mutant RC genes to produce mutant RC proteins. Preliminary characterization of a site-directed mutant at Tyr L222 in the QB binding domain of the RC is also presented.

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References

  1. Wraight, CA. (1981) Israel J. Chem. 21,348–354.

    CAS  Google Scholar 

  2. Michel, H., Epp, O., and Deisenhofer, J. (1986) EMBO J. 5,2445–2451.

    PubMed  CAS  Google Scholar 

  3. Allen, J.P., Feher, G., Yeates, T.O., Komiya, H., and Reese, D.C. (1987) Proc. Natl. Acad. Sci. USA 84,6162–6166.

    Article  PubMed  CAS  Google Scholar 

  4. Stein, R.R., Castellvi, A.L., Bogacz, J.P., and Wraight, CA. (1984) J. Cell. Biochem. 24,243–259.

    Article  PubMed  CAS  Google Scholar 

  5. Paddock, M.L., Rongey, S.H., Abresch, E.C., Feher, G. and Okamura, M.Y. (1988) Photosynthesis Res. 17,75–96.

    Article  CAS  Google Scholar 

  6. Williams, J.C., Steiner, LA. and Feher, G. (1986) Proteins 1,312–325.

    Article  PubMed  CAS  Google Scholar 

  7. Simon, R, Preifer, U. and Puhler, A. (1983) Biotechnology 1:784–791.

    Article  CAS  Google Scholar 

  8. Davis, J., Donohue, T.J. and Kaplan, S. (1988) J. Bacteriol. 170,320–329.

    PubMed  CAS  Google Scholar 

  9. Mead, DA, Szczena-Scorupa, E., and Kemper, B. (1986) Protein Engineering 1:67–74.

    Article  PubMed  CAS  Google Scholar 

  10. Kunkle, TA. (1987) in Current protocols in molecular biology (Ausubel, F.M. et al. eds.) pp. 8.8.1.–8.8.6. John Wiley and Sons, New York.

    Google Scholar 

  11. Ditta, G., Schmidhauser, T., Yakobson, E., Lu, P., Iiang, X-W., Finlay, D.R., Guiney, D. and Helinski, D.R. (1985) 13,149–153.

    Google Scholar 

  12. Jolchine, G. and Reiss-Husson, F. (1974) FEBS Lett. 40,5–8.

    Article  PubMed  CAS  Google Scholar 

  13. Allen, J.P., Feher, G., Yeates, T.O., Komiya, H., and Reese, D.C. (1988) Proc. Natl. Acad. Sci. USA 85,8487–8491.

    Article  PubMed  CAS  Google Scholar 

  14. Paddock, M.L., Rongey, S.H., Feher, G., and Okamura, M.Y. (1989) Proc. Acad. Sci. USA, in press.

    Google Scholar 

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Takahashi, E., Maroti, P., Wraight, C.A. (1990). Site-Directed Mutagenesis of Rhodobacter sphaeroides Reaction Center: The Role of Tyrosine L222. In: Baltscheffsky, M. (eds) Current Research in Photosynthesis. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-0511-5_36

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  • DOI: https://doi.org/10.1007/978-94-009-0511-5_36

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-010-6716-4

  • Online ISBN: 978-94-009-0511-5

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