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Protein translocation

Surfing the channel

Nature Reviews Molecular Cell Biology volume 9, pages 922–923 (2008)Cite this article

A single copy of the SecY complex forms an hourglass-shaped channel with a pore ring constriction midway across the membrane. The complex consists of two halves that are linked on the back and form a lateral gate at the front to allow release of transmembrane domains into the plasma membrane. In the closed state, the channel is blocked at the extracellular side of the pore ring by a short helix called the plug domain. In the open state, binding of a signal sequence or transmembrane domain of a translocating substrate to the lateral gate displaces the plug, which allows translocation to proceed. The driving force for translocation of polypeptides across the membrane depends on association of the translocon with different partners. Interaction with ribosomes allows co-translational translocation of emerging polypeptides, whereas post-translational translocation of fully synthesized polypeptides in bacteria requires binding to SecA.

...PPXD and NBD2 form a clamp that captures and aligns substrates for insertion into the pore.

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ORIGINAL RESEARCH PAPERS

  1. Zimmer, J. et al. Structure of a complex of the ATPase SecA and the protein-translocation channel. Nature 455, 936–943 (2008)

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  2. Erlandson, K. J. et al. A role for the two-helix finger of the SecA ATPase in protein translocation. Nature 455, 984–987 (2008)

    Article  CAS  Google Scholar 

  3. Tsukazaki, T. et al. Conformational transition of Sec machinery inferred from bacterial SecYE structures. Nature 455, 988–991 (2008)

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  1. Associate Editor, Nature Reviews Microbiology,

    Andrew Jermy

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  1. Andrew Jermy
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Jermy, A. Surfing the channel. Nat Rev Mol Cell Biol 9, 922–923 (2008). https://doi.org/10.1038/nrm2547

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