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Translocation of preproteins across the  Escherichia coli  inner membrane requires anionic lipids by virtue of their negative head-group charge either  in vivo  or  in situ . However, available results do not differentiate between the roles of monoanionic phosphatidylglycerol and dianionic cardiolipin (CL) in this essential membrane-related process. To define  in vivo  the molecular steps affected by the absence of CL in protein translocation and insertion, we analyzed translocon activity, SecYEG stability and its interaction with SecA in an  E. coli  mutant devoid of CL. Although no growth defects were observed, co- and post-translational translocation of α-helical proteins across inner membrane and the assembly of outer membrane β-barrel precursors were severely compromised in CL-lacking cells. Components of proton-motive force which could impair protein insertion into and translocation across the inner membrane, were unaffected. However, stability of the dimeric SecYEG complex and oligomerization properties of SecA were strongly compromised while the levels of individual SecYEG translocon components, SecA and insertase YidC were largely unaffected. These results demonstrate that CL is required  in vivo  for the stability of the bacterial translocon and its efficient function in co-translational insertion into and translocation across the inner membrane of  E. coli .

Cardiolipin is required in vivo for the stability of bacterial translocon and optimal membrane protein translocation and insertion