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Disulfide bridge formation between SecY and a translocating polypeptide localizes the translocation pore to the center of SecY

Howard Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, Boston, MA 02115

Correspondence to Tom A. Rapoport: tom_rapoport{at}hms.harvard.edu

Abstract

During their biosynthesis, many proteins pass through the membrane via a hydrophilic channel formed by the heterotrimeric Sec61/SecY complex. Whether this channel forms at the interface of multiple copies of Sec61/SecY or is intrinsic to a monomeric complex, as suggested by the recently solved X-ray structure of the Methanococcus jannaschii SecY complex, is a matter of contention. By introducing a single cysteine at various positions in Escherichia coli SecY and testing its ability to form a disulfide bond with a single cysteine in a translocating chain, we provide evidence that translocating polypeptides pass through the center of the SecY complex. The strongest cross-links were observed with residues that would form a constriction in an hourglass-shaped pore. This suggests that the channel makes only limited contact with a translocating polypeptide, thus minimizing the energy required for translocation.

Abbreviation used in this paper: TM, transmembrane.

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