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Structural biology

Clamour for a kiss

Nature volume 455, pages 879–880 (2008)Cite this article

Precisely how proteins snake their way through channels in cell membranes is unclear. Complexes between the SecY channel and its motor protein, and the use of a 'molecular endoscope', provide fascinating clues.

To cross cellular membranes, secretory proteins use specialized channels such as that known as SecY. When ribosomes start synthesizing secretory proteins, the ribosome–protein complex is hijacked to the mouth of SecY. There the nascent 'pre-protein' chains, which carry specific recognition tags known as signal peptides, are threaded through the endoplasmic reticulum — a membranous mesh inside the cells of eukaryotic organisms — or through the plasma membrane that surrounds prokaryotic cells such as bacteria. In bacteria, a 'push' motor called SecA can also mediate ribosome-independent protein secretion through SecY channels, using the cell's energy currency ATP in the process. The structure of such cellular machines dictates their function and so can be highly informative. But despite having known for some time1,2 what the separated parts — SecY and SecA — look like, we are no wiser about what they look like when united. In this issue, three studies3,4,5 provide eagerly awaited snapshots of how the SecY channel and the SecA motor come together in a 'kissing' complex, and how they might move to mediate protein translocation.

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Figure 1: Protein translocation in bacterial cells.

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Authors and Affiliations

  1. and in the Department of Biology, Anastassios Economou is at the Institute of Molecular Biology and Biotechnology, Foundation of Research and Technology-Hellas, University of Crete, PO Box 1385, Iraklio, Crete, Greece. aeconomo@imbb.forth.gr,

    Anastassios Economou

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  1. Anastassios Economou
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Economou, A. Clamour for a kiss. Nature 455, 879–880 (2008). https://doi.org/10.1038/455879a

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