AI Article Synopsis
- The GspD secretin is crucial for the bacterial type II secretion system (T2SS) that releases harmful proteins or toxins linked to diseases like diarrhea and cholera.
- The research focuses on the translocation process of two types of GspD secretins, using advanced imaging techniques to understand their structures during this process.
- Findings reveal that the two GspD variants have different interactions with the membrane and methods of crossing the peptidoglycan layer, leading to distinct models for how they function in T2SS assembly.
Article Abstract
The GspD secretin is the outer membrane channel of the bacterial type II secretion system (T2SS) which secrets diverse effector proteins or toxins that cause severe diseases such as diarrhea and cholera. GspD needs to translocate from the inner to the outer membrane to exert its function, and this process is an essential step for T2SS to assemble. Here, we investigate two types of secretins discovered so far in , GspD and GspD , respectively. By electron cryotomography subtomogram averaging, we determine structures of all the key intermediate states of GspD and GspD in the translocation process, with resolution ranging from 9 Å to 19 Å. In our results, GspD and GspD present entirely different membrane interaction patterns and ways of going across the peptidoglycan layer. We propose two distinct models for the membrane translocation of GspD and GspD , providing a comprehensive perspective on the inner to outer membrane biogenesis of T2SS secretins.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9882097 | PMC |
| http://dx.doi.org/10.1101/2023.01.10.523476 | DOI Listing |
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