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YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli
Author(s) -
Malinverni Juliana C.,
Werner John,
Kim Seokhee,
Sklar Joseph G.,
Kahne Daniel,
Misra Rajeev,
Silhavy Thomas J.
Publication year - 2006
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2006.05211.x
Subject(s) - bacterial outer membrane , biology , escherichia coli , protein folding , bacteria , folding (dsp implementation) , membrane protein , microbiology and biotechnology , membrane , biochemistry , genetics , gene , engineering , electrical engineering
Summary Recent advances in the study of bacterial membranes have led to the identification of a multicomponent YaeT complex in the outer membrane (OM) of Gram‐negative bacteria that is involved in the targeting and folding of β‐barrel outer membrane proteins (OMPs). In Escherichia coli , this complex consists of an essential OMP, YaeT, and three OM lipoproteins, YfgL, NlpB and YfiO. YfiO is the only essential lipoprotein component of the complex. We show that this lipoprotein is required for the proper assembly and/or targeting of OMPs to the OM but not the assembly of lipopolysaccharides (LPS). Depletion of YfiO causes similar phenotypes as does the depletion of YaeT, and we conclude that YfiO plays a critical role in YaeT‐mediated OMP folding. We demonstrate that YfiO and YfgL directly interact with YaeT in vitro , while NlpB interacts directly with YfiO. Genetic analysis verifies the importance of YfiO and its interactions with NlpB in maintaining the functional integrity of the YaeT complex.