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Reconstitution of the Catalytic Core of F-ATPase (αβ)3γ from Escherichia coli Using Chemically Synthesized Subunit γ

Authors

  • Frank Wintermann,

    Corresponding author
    1. Universität Osnabrück, Fachbereich Biologie/Chemie, Abt. Biochemie, Barbarastrasse 13, 49076 Osnabrück (Germany)
    • Universität Osnabrück, Fachbereich Biologie/Chemie, Abt. Biochemie, Barbarastrasse 13, 49076 Osnabrück (Germany)
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  • Siegfried Engelbrecht

    Corresponding author
    1. Universität Osnabrück, Fachbereich Biologie/Chemie, Abt. Biochemie, Barbarastrasse 13, 49076 Osnabrück (Germany)
    • Universität Osnabrück, Fachbereich Biologie/Chemie, Abt. Biochemie, Barbarastrasse 13, 49076 Osnabrück (Germany)
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Errata

This article is corrected by:

  1. Errata: Corrigendum: Reconstitution of the Catalytic Core of F-ATPase (αβ)3γ from Escherichia coli Using Chemically Synthesized Subunit γ Volume 52, Issue 18, 4715, Article first published online: 21 April 2013

  • We thank Martin Engelhard and Marc Dittmann (both MPI Dortmund (Germany)) for discussions and support, especially use of their HF apparatus and other lab facilities. Special thanks to Stephen Kent and Kalyaneswar Mandel (both University of Chicago) for support and a generous gift of PAM resin, several test peptides, and a most enjoyable stay in the lab (F.W.). We thank Julia Paul for preliminary experiments regarding the preparation of subunits α and β, André Wächter for a sample of over-expressed subunit γ, and Oliver Pänke (all then University of Osnabrück (Germany)) for discussions. Special thanks to Stefan Walter for support with MS measurements and to Wolfgang Junge and Christian Ungermann for support (all University of Osnabrück). Financial support from the Deutsche Forschungsgemeinschaft (SFB 431) and the European Community (Nanomot project) is gratefully acknowledged. F.W. acknowledges an EMBO short-term fellowship (ASTF 225-2009) which funded a stay in the Kent lab.

Abstract

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Hooking up: Subunit γ of an F-ATPase with 11 point mutations was ligated chemically from six peptides and then reconstituted with further subunits of the (αβ)3γ catalytic core complex. The biologically active protein with 286 residues currently represents the longest nonredundant polypeptide chain synthesized by chemical means. The yields of the five consecutive ligations, especially the last three, dropped the total yield to only 0.005 %.

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