A unifying mechanism for protein transport through the core bacterial Sec machinery
Encapsulation and compartmentalization are fundamental to the evolution of cellular life, but they also pose a challenge: how to partition the molecules that perform biological functions—the proteins—across impermeable barriers into sub-cellular organelles, and to the outside. The solution lies in t...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
| Published: |
The Royal Society
2023-08-01
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| Series: | Open Biology |
| Subjects: | |
| Online Access: | https://royalsocietypublishing.org/doi/10.1098/rsob.230166 |
| _version_ | 1797733213852925952 |
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| author | William J. Allen Ian Collinson |
| author_facet | William J. Allen Ian Collinson |
| author_sort | William J. Allen |
| collection | DOAJ |
| description | Encapsulation and compartmentalization are fundamental to the evolution of cellular life, but they also pose a challenge: how to partition the molecules that perform biological functions—the proteins—across impermeable barriers into sub-cellular organelles, and to the outside. The solution lies in the evolution of specialized machines, translocons, found in every biological membrane, which act both as gate and gatekeeper across and into membrane bilayers. Understanding how these translocons operate at the molecular level has been a long-standing ambition of cell biology, and one that is approaching its denouement; particularly in the case of the ubiquitous Sec system. In this review, we highlight the fruits of recent game-changing technical innovations in structural biology, biophysics and biochemistry to present a largely complete mechanism for the bacterial version of the core Sec machinery. We discuss the merits of our model over alternative proposals and identify the remaining open questions. The template laid out by the study of the Sec system will be of immense value for probing the many other translocons found in diverse biological membranes, towards the ultimate goal of altering or impeding their functions for pharmaceutical or biotechnological purposes. |
| first_indexed | 2024-03-12T12:24:53Z |
| format | Article |
| id | doaj.art-9e1a9da24031489282e8f6a1fb944ce7 |
| institution | Directory Open Access Journal |
| issn | 2046-2441 |
| language | English |
| last_indexed | 2024-03-12T12:24:53Z |
| publishDate | 2023-08-01 |
| publisher | The Royal Society |
| record_format | Article |
| series | Open Biology |
| spelling | doaj.art-9e1a9da24031489282e8f6a1fb944ce72023-08-29T23:05:28ZengThe Royal SocietyOpen Biology2046-24412023-08-0113810.1098/rsob.230166A unifying mechanism for protein transport through the core bacterial Sec machineryWilliam J. Allen0Ian Collinson1School of Biochemistry, University of Bristol, Bristol BS8 1TD, UKSchool of Biochemistry, University of Bristol, Bristol BS8 1TD, UKEncapsulation and compartmentalization are fundamental to the evolution of cellular life, but they also pose a challenge: how to partition the molecules that perform biological functions—the proteins—across impermeable barriers into sub-cellular organelles, and to the outside. The solution lies in the evolution of specialized machines, translocons, found in every biological membrane, which act both as gate and gatekeeper across and into membrane bilayers. Understanding how these translocons operate at the molecular level has been a long-standing ambition of cell biology, and one that is approaching its denouement; particularly in the case of the ubiquitous Sec system. In this review, we highlight the fruits of recent game-changing technical innovations in structural biology, biophysics and biochemistry to present a largely complete mechanism for the bacterial version of the core Sec machinery. We discuss the merits of our model over alternative proposals and identify the remaining open questions. The template laid out by the study of the Sec system will be of immense value for probing the many other translocons found in diverse biological membranes, towards the ultimate goal of altering or impeding their functions for pharmaceutical or biotechnological purposes.https://royalsocietypublishing.org/doi/10.1098/rsob.230166protein transportbacterial secretionSec machinerySecYEGSecA |
| spellingShingle | William J. Allen Ian Collinson A unifying mechanism for protein transport through the core bacterial Sec machinery Open Biology protein transport bacterial secretion Sec machinery SecYEG SecA |
| title | A unifying mechanism for protein transport through the core bacterial Sec machinery |
| title_full | A unifying mechanism for protein transport through the core bacterial Sec machinery |
| title_fullStr | A unifying mechanism for protein transport through the core bacterial Sec machinery |
| title_full_unstemmed | A unifying mechanism for protein transport through the core bacterial Sec machinery |
| title_short | A unifying mechanism for protein transport through the core bacterial Sec machinery |
| title_sort | unifying mechanism for protein transport through the core bacterial sec machinery |
| topic | protein transport bacterial secretion Sec machinery SecYEG SecA |
| url | https://royalsocietypublishing.org/doi/10.1098/rsob.230166 |
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