Cryo-electron microscopic structure of SecA protein bound to the 70S ribosome
SecA is an ATP-dependent molecular motor pumping secretory and outer membrane proteins across the cytoplasmic membrane in bacteria. SecA associates with the protein-conducting channel, the heterotrimeric SecYEG complex, in a so-called posttranslational manner. A recent study further showed binding o...
| Main Authors: | , , , , , , , , , |
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| Format: | Journal Article |
| Language: | English |
| Published: |
2018
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| Online Access: | https://hdl.handle.net/10356/88409 http://hdl.handle.net/10220/45804 |
| _version_ | 1826112873873539072 |
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| author | Singh, Rajkumar Kraft, Christian Jaiswal, Rahul Sejwal, Kushal Kasaragod, Vikram Babu Kuper, Jochen Bürger, Jörg Mielke, Thorsten Luirink, Joen Bhushan, Shashi |
| author2 | School of Biological Sciences |
| author_facet | School of Biological Sciences Singh, Rajkumar Kraft, Christian Jaiswal, Rahul Sejwal, Kushal Kasaragod, Vikram Babu Kuper, Jochen Bürger, Jörg Mielke, Thorsten Luirink, Joen Bhushan, Shashi |
| author_sort | Singh, Rajkumar |
| collection | NTU |
| description | SecA is an ATP-dependent molecular motor pumping secretory and outer membrane proteins across the cytoplasmic membrane in bacteria. SecA associates with the protein-conducting channel, the heterotrimeric SecYEG complex, in a so-called posttranslational manner. A recent study further showed binding of a monomeric state of SecA to the ribosome. However, the true oligomeric state of SecA remains controversial because SecA can also form functional dimers, and high-resolution crystal structures exist for both the monomer and the dimer. Here we present the cryo-electron microscopy structures of Escherichia coli SecA bound to the ribosome. We show that not only a monomeric SecA binds to the ribosome but also that two copies of SecA can be observed that form an elongated dimer. Two copies of SecA completely surround the tunnel exit, providing a unique environment to the nascent polypeptides emerging from the ribosome. We identified the N-terminal helix of SecA required for a stable association with the ribosome. The structures indicate a possible function of the dimeric form of SecA at the ribosome. |
| first_indexed | 2024-10-01T03:14:14Z |
| format | Journal Article |
| id | ntu-10356/88409 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T03:14:14Z |
| publishDate | 2018 |
| record_format | dspace |
| spelling | ntu-10356/884092023-02-28T17:02:27Z Cryo-electron microscopic structure of SecA protein bound to the 70S ribosome Singh, Rajkumar Kraft, Christian Jaiswal, Rahul Sejwal, Kushal Kasaragod, Vikram Babu Kuper, Jochen Bürger, Jörg Mielke, Thorsten Luirink, Joen Bhushan, Shashi School of Biological Sciences Electron Microscopy Protein Secretion DRNTU::Science::Biological sciences SecA is an ATP-dependent molecular motor pumping secretory and outer membrane proteins across the cytoplasmic membrane in bacteria. SecA associates with the protein-conducting channel, the heterotrimeric SecYEG complex, in a so-called posttranslational manner. A recent study further showed binding of a monomeric state of SecA to the ribosome. However, the true oligomeric state of SecA remains controversial because SecA can also form functional dimers, and high-resolution crystal structures exist for both the monomer and the dimer. Here we present the cryo-electron microscopy structures of Escherichia coli SecA bound to the ribosome. We show that not only a monomeric SecA binds to the ribosome but also that two copies of SecA can be observed that form an elongated dimer. Two copies of SecA completely surround the tunnel exit, providing a unique environment to the nascent polypeptides emerging from the ribosome. We identified the N-terminal helix of SecA required for a stable association with the ribosome. The structures indicate a possible function of the dimeric form of SecA at the ribosome. Published version 2018-09-04T02:36:04Z 2019-12-06T17:02:41Z 2018-09-04T02:36:04Z 2019-12-06T17:02:41Z 2014 Journal Article Singh, R., Kraft, C., Jaiswal, R., Sejwal, K., Kasaragod, V. B., Kuper, J., . . . Bhusan, S. (2014). Cryo-electron microscopic structure of SecA protein bound to the 70S ribosome. Journal of Biological Chemistry, 289(10), 7190-7199. doi:10.1074/jbc.M113.506634 0021-9258 https://hdl.handle.net/10356/88409 http://hdl.handle.net/10220/45804 10.1074/jbc.M113.506634 24443566 en Journal of Biological Chemistry © 2014 The American Society for Biochemistry and Molecular Biology, Inc. This paper was published in Journal of Biological Chemistry and is made available as an electronic reprint (preprint) with permission of The American Society for Biochemistry and Molecular Biology, Inc. The published version is available at: [http://dx.doi.org/10.1074/jbc.M113.506634]. One print or electronic copy may be made for personal use only. Systematic or multiple reproduction, distribution to multiple locations via electronic or other means, duplication of any material in this paper for a fee or for commercial purposes, or modification of the content of the paper is prohibited and is subject to penalties under law. 13 p. application/pdf |
| spellingShingle | Electron Microscopy Protein Secretion DRNTU::Science::Biological sciences Singh, Rajkumar Kraft, Christian Jaiswal, Rahul Sejwal, Kushal Kasaragod, Vikram Babu Kuper, Jochen Bürger, Jörg Mielke, Thorsten Luirink, Joen Bhushan, Shashi Cryo-electron microscopic structure of SecA protein bound to the 70S ribosome |
| title | Cryo-electron microscopic structure of SecA protein bound to the 70S ribosome |
| title_full | Cryo-electron microscopic structure of SecA protein bound to the 70S ribosome |
| title_fullStr | Cryo-electron microscopic structure of SecA protein bound to the 70S ribosome |
| title_full_unstemmed | Cryo-electron microscopic structure of SecA protein bound to the 70S ribosome |
| title_short | Cryo-electron microscopic structure of SecA protein bound to the 70S ribosome |
| title_sort | cryo electron microscopic structure of seca protein bound to the 70s ribosome |
| topic | Electron Microscopy Protein Secretion DRNTU::Science::Biological sciences |
| url | https://hdl.handle.net/10356/88409 http://hdl.handle.net/10220/45804 |
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