Fine interaction profiling of VemP and mechanisms responsible for its translocation-coupled arrest-cancelation
Bacterial cells utilize monitoring substrates, which undergo force-sensitive translation elongation arrest, to feedback-regulate a Sec-related gene. Vibrio alginolyticus VemP controls the expression of SecD/F that stimulates a late step of translocation by undergoing export-regulated elongation arre...
| Main Authors: | , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
eLife Sciences Publications Ltd
2020-12-01
|
| Series: | eLife |
| Subjects: | |
| Online Access: | https://elifesciences.org/articles/62623 |
| _version_ | 1811253155678126080 |
|---|---|
| author | Ryoji Miyazaki Yoshinori Akiyama Hiroyuki Mori |
| author_facet | Ryoji Miyazaki Yoshinori Akiyama Hiroyuki Mori |
| author_sort | Ryoji Miyazaki |
| collection | DOAJ |
| description | Bacterial cells utilize monitoring substrates, which undergo force-sensitive translation elongation arrest, to feedback-regulate a Sec-related gene. Vibrio alginolyticus VemP controls the expression of SecD/F that stimulates a late step of translocation by undergoing export-regulated elongation arrest. Here, we attempted at delineating the pathway of the VemP nascent-chain interaction with Sec-related factors, and identified the signal recognition particle (SRP) and PpiD (a membrane-anchored periplasmic chaperone) in addition to other translocon components and a ribosomal protein as interacting partners. Our results showed that SRP is required for the membrane-targeting of VemP, whereas PpiD acts cooperatively with SecD/F in the translocation and arrest-cancelation of VemP. We also identified the conserved Arg-85 residue of VemP as a crucial element that confers PpiD-dependence to VemP and plays an essential role in the regulated arrest-cancelation. We propose a scheme of the arrest-cancelation processes of VemP, which likely monitors late steps in the protein translocation pathway. |
| first_indexed | 2024-04-12T16:46:30Z |
| format | Article |
| id | doaj.art-d8ee50a4235c43a3af1c6a76c205d09d |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-12T16:46:30Z |
| publishDate | 2020-12-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-d8ee50a4235c43a3af1c6a76c205d09d2022-12-22T03:24:35ZengeLife Sciences Publications LtdeLife2050-084X2020-12-01910.7554/eLife.62623Fine interaction profiling of VemP and mechanisms responsible for its translocation-coupled arrest-cancelationRyoji Miyazaki0Yoshinori Akiyama1https://orcid.org/0000-0003-4483-5408Hiroyuki Mori2https://orcid.org/0000-0002-0429-1269Institute for Frontier Life and Medical Sciences, Kyoto University, Kyoto, JapanInstitute for Frontier Life and Medical Sciences, Kyoto University, Kyoto, JapanInstitute for Frontier Life and Medical Sciences, Kyoto University, Kyoto, JapanBacterial cells utilize monitoring substrates, which undergo force-sensitive translation elongation arrest, to feedback-regulate a Sec-related gene. Vibrio alginolyticus VemP controls the expression of SecD/F that stimulates a late step of translocation by undergoing export-regulated elongation arrest. Here, we attempted at delineating the pathway of the VemP nascent-chain interaction with Sec-related factors, and identified the signal recognition particle (SRP) and PpiD (a membrane-anchored periplasmic chaperone) in addition to other translocon components and a ribosomal protein as interacting partners. Our results showed that SRP is required for the membrane-targeting of VemP, whereas PpiD acts cooperatively with SecD/F in the translocation and arrest-cancelation of VemP. We also identified the conserved Arg-85 residue of VemP as a crucial element that confers PpiD-dependence to VemP and plays an essential role in the regulated arrest-cancelation. We propose a scheme of the arrest-cancelation processes of VemP, which likely monitors late steps in the protein translocation pathway.https://elifesciences.org/articles/62623Vibrioprotein exportnascent chainSecYSecGFfh |
| spellingShingle | Ryoji Miyazaki Yoshinori Akiyama Hiroyuki Mori Fine interaction profiling of VemP and mechanisms responsible for its translocation-coupled arrest-cancelation eLife Vibrio protein export nascent chain SecY SecG Ffh |
| title | Fine interaction profiling of VemP and mechanisms responsible for its translocation-coupled arrest-cancelation |
| title_full | Fine interaction profiling of VemP and mechanisms responsible for its translocation-coupled arrest-cancelation |
| title_fullStr | Fine interaction profiling of VemP and mechanisms responsible for its translocation-coupled arrest-cancelation |
| title_full_unstemmed | Fine interaction profiling of VemP and mechanisms responsible for its translocation-coupled arrest-cancelation |
| title_short | Fine interaction profiling of VemP and mechanisms responsible for its translocation-coupled arrest-cancelation |
| title_sort | fine interaction profiling of vemp and mechanisms responsible for its translocation coupled arrest cancelation |
| topic | Vibrio protein export nascent chain SecY SecG Ffh |
| url | https://elifesciences.org/articles/62623 |
| work_keys_str_mv | AT ryojimiyazaki fineinteractionprofilingofvempandmechanismsresponsibleforitstranslocationcoupledarrestcancelation AT yoshinoriakiyama fineinteractionprofilingofvempandmechanismsresponsibleforitstranslocationcoupledarrestcancelation AT hiroyukimori fineinteractionprofilingofvempandmechanismsresponsibleforitstranslocationcoupledarrestcancelation |