National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
R01GM143380
米国
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)
R01HL162842
米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
R01GM080139
米国
Cancer Prevention and Research Institute of Texas (CPRIT)
RP190602
米国
引用
ジャーナル: Nat Commun / 年: 2023 タイトル: Membrane translocation process revealed by in situ structures of type II secretion system secretins. 著者: Zhili Yu / Yaoming Wu / Muyuan Chen / Tong Huo / Wei Zheng / Steven J Ludtke / Xiaodong Shi / Zhao Wang / 要旨: The GspD secretin is the outer membrane channel of the bacterial type II secretion system (T2SS) which secrets diverse toxins that cause severe diseases such as diarrhea and cholera. GspD needs to ...The GspD secretin is the outer membrane channel of the bacterial type II secretion system (T2SS) which secrets diverse 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 Escherichia coli, GspD, and GspD. By electron cryotomography subtomogram averaging, we determine in situ structures of 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 transitioning the peptidoglycan layer. From this, we hypothesize 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.