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Both An N-Terminal 65-Kda Domain And A C-Terminal 30-Kda Domain Of Seca Cycle Into The Membrane At Secyeg During Translocation, Jerry Eichler, William Wickner

Dartmouth Scholarship

SecA, a 102-kDa hydrophilic protein, couples the energy of ATP binding to the translocation of preprotein across the bacterial inner membrane. SecA function and topology were studied with metabolically labeled [35S]SecA and with inner membrane vesicles from cells that overex- pressed SecYEGDFyajC, the integral domain of preprotein translocase. During translocation in the presence of ATP and preprotein, a 65-kDa N-terminal domain of SecA is protected from proteolytic digestion through insertion into the mem- brane, as previously reported for a 30-kDa C-terminal domain [Economou, A. & Wickner, W. (1994) Cell 78, 835–843]. Insertion of both domains occurs at saturable SecYEGDFyajC sites …

Robert J. Boxer Papers, Zach S. Henderson Library Special Collections

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This collection consists of various drafts and the finished manuscript of Robert J. Boxer's 1997 textbook, Essentials of Organic Chemistry. Materials span 1988- 1997 and also include correspondence with publishers, including contracts.

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