ArticleProceedings of the National Academy of Sciences of the United States of America2025
A fluorescent reporter and single-turnover kinetics reveal insight into BAM complex function.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
The β-barrel assembly machine (BAM) is an essential protein complex that folds and inserts outer membrane β-barrel proteins (OMPs) into the bacterial outer membrane. The BAM complex contains the essential BamA OMP with five soluble polypeptide transport-associated (POTRA) domains, which scaffold the essential BamD lipoprotein and the nonessential lipoproteins BamB/C/E. The importance of each BAM component has been investigated primarily using cell-based phenotypic assays, and structural data have revealed insights into the role of the BamA β-barrel in OMP folding. However, in vitro quantitative analysis for the function of each BAM component has been challenging. We describe the development of a fluorescent reporter of OMP folding, bOmpA-A488, which we use to obtain single-turnover kinetic parameters for wild-type BAM complex in vitro. We observe a k
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