AFM observation of protein translocation mediated by one unit of SecYEG-SecA complex

Yui Kanaoka, Takaharu Mori (), Wataru Nagaike, Seira Itaya, Yuto Nonaka, Hidetaka Kohga, Takamitsu Haruyama, Yasunori Sugano, Ryoji Miyazaki, Muneyoshi Ichikawa, Takayuki Uchihashi () and Tomoya Tsukazaki ()
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Yui Kanaoka: Nagoya University
Takaharu Mori: Tokyo University of Science
Wataru Nagaike: Nagoya University
Seira Itaya: Nara Institute of Science and Technology
Yuto Nonaka: Nagoya University
Hidetaka Kohga: Nara Institute of Science and Technology
Takamitsu Haruyama: Nara Institute of Science and Technology
Yasunori Sugano: Nara Institute of Science and Technology
Ryoji Miyazaki: Nara Institute of Science and Technology
Muneyoshi Ichikawa: Fudan University
Takayuki Uchihashi: Nagoya University
Tomoya Tsukazaki: Nara Institute of Science and Technology

Nature Communications, 2025, vol. 16, issue 1, 1-12

Abstract: Abstract Protein translocation across cellular membranes is an essential and nano-scale dynamic process. In the bacterial cytoplasmic membrane, the core proteins in this process are a membrane protein complex, SecYEG, corresponding to the eukaryotic Sec61 complex, and a cytoplasmic protein, SecA ATPase. Despite more than three decades of extensive research on Sec proteins, from genetic experiments to cutting-edge single-molecule analyses, no study has visually demonstrated protein translocation. Here, we visualize the translocation, via one unit of a SecYEG-SecA-embedded nanodisc, of an unfolded substrate protein by high-speed atomic force microscopy (HS-AFM). Additionally, the uniform unidirectional distribution of nanodiscs on a mica substrate enables the HS-AFM image data analysis, revealing dynamic structural changes in the polypeptide-crosslinking domain of SecA between wide-open and closed states depending on nucleotides. The nanodisc-AFM approach will allow us to execute detailed analyses of Sec proteins as well as visualize nano-scale events of other membrane proteins.

Date: 2025
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DOI: 10.1038/s41467-024-54875-x

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