GFT projection NMR based resonance assignment of membrane proteins: application to subunit c of E. coli F1F0 ATP synthase in LPPG micelles

2008 ◽  
Vol 40 (3) ◽  
pp. 157-163 ◽  
Author(s):  
Qi Zhang ◽  
Hanudatta S. Atreya ◽  
Douglas E. Kamen ◽  
Mark E. Girvin ◽  
Thomas Szyperski
2004 ◽  
Vol 165 (2) ◽  
pp. 213-222 ◽  
Author(s):  
Martin van der Laan ◽  
Philipp Bechtluft ◽  
Stef Kol ◽  
Nico Nouwen ◽  
Arnold J.M. Driessen

The Escherichia coli YidC protein belongs to the Oxa1 family of membrane proteins that have been suggested to facilitate the insertion and assembly of membrane proteins either in cooperation with the Sec translocase or as a separate entity. Recently, we have shown that depletion of YidC causes a specific defect in the functional assembly of F1F0 ATP synthase and cytochrome o oxidase. We now demonstrate that the insertion of in vitro–synthesized F1F0 ATP synthase subunit c (F0c) into inner membrane vesicles requires YidC. Insertion is independent of the proton motive force, and proteoliposomes containing only YidC catalyze the membrane insertion of F0c in its native transmembrane topology whereupon it assembles into large oligomers. Co-reconstituted SecYEG has no significant effect on the insertion efficiency. Remarkably, signal recognition particle and its membrane-bound receptor FtsY are not required for the membrane insertion of F0c. In conclusion, a novel membrane protein insertion pathway in E. coli is described in which YidC plays an exclusive role.


2010 ◽  
Vol 48 (1) ◽  
pp. 1-11 ◽  
Author(s):  
Yasuto Todokoro ◽  
Masatoshi Kobayashi ◽  
Takeshi Sato ◽  
Toru Kawakami ◽  
Ikuko Yumen ◽  
...  

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