ArticleMolecular microbiology2017
Structural basis for substrate selection by the translocation and assembly module of the β-barrel assembly machinery.
Article in Molecular microbiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- The Omp85 family protein, TamA, exhibits characteristics of a suitable drug target againstMicrobiology (Reading, England) · 2026Article
- The translocation assembly module (TAM) catalyzes the assembly of bacterial outer membrane proteins in vitro.Nature communications · 2024Article
- POTRA domains of the TamA insertase interact with the outer membrane and modulate membrane properties.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The translocation assembly module (TAM) catalyzes the assembly of bacterial outer membrane proteinsbioRxiv : the preprint server for biology · 2024Article
- The TAM, a Translocation and Assembly Module for protein assembly and potential conduit for phospholipid transfer.EMBO reports · 2024Review
- Redundant essentiality of AsmA-like proteins inmSphere · 2024Article
- ATP-independent assembly machinery of bacterial outer membranes: BAM complex structure and function set the stage for next-generation therapeutics.Protein science : a publication of the Protein Society · 2024Review
- A conserved C-terminal domain of TamB interacts with multiple BamA POTRA domains in Borreliella burgdorferi.PloS one · 2024Article
- TamAB is regulated by PhoPQ and functions in outer membrane homeostasis duringJournal of bacteriology · 2023Article
- Dynamic interplay between the periplasmic chaperone SurA and the BAM complex in outer membrane protein folding.Communications biology · 2022Article
- A noncanonical chaperone interacts with drug efflux pumps during their assembly into bacterial outer membranes.PLoS biology · 2022Article
- Folding Control in the Path of Type 5 Secretion.Toxins · 2021Review
- TAM mediates adaptation of carbapenem-resistant Klebsiella pneumoniae to antimicrobial stress during host colonization and infection.PLoS pathogens · 2021Article
- Backbone Hydrogen Bond Energies in Membrane Proteins Are Insensitive to Large Changes in Local Water Concentration.Journal of the American Chemical Society · 2020Article
- Presence of substrate aids lateral gate separation in LptD.Biochimica et biophysica acta. Biomembranes · 2020Article
- Article
- Chaperone OsmY facilitates the biogenesis of a major family of autotransporters.Molecular microbiology · 2019Article
- Article
- The Rich Tapestry of Bacterial Protein Translocation Systems.The protein journal · 2019Review
- Type V Secretion in Gram-Negative Bacteria.EcoSal Plus · 2019Article
Corrections and comments
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Authors and funding
13 authors.
Funding
Abstract
The assembly of proteins into bacterial outer membranes is a key cellular process that we are only beginning to understand, mediated by the β-barrel assembly machinery (BAM). Two crucial elements of that machinery are the core BAM complex and the translocation and assembly module (TAM), with each containing a member of the Omp85 superfamily of proteins: BamA in the BAM complex, TamA in the TAM. Here, we used the substrate protein FimD as a model to assess the selectivity of substrate interactions for the TAM relative to those of the BAM complex. A peptide scan revealed that TamA and BamA bind the β-strands of FimD, and do so selectively. Chemical cross-linking and molecular dynamics are consistent with this interaction taking place between the first and last strand of the TamA barrel domain, providing the first experimental evidence of a lateral gate in TamA: a structural element implicated in membrane protein assembly. We suggest that the lateral gates in TamA and BamA provide different environments for substrates to engage, with the differences observed here beginning to address how the TAM can be more effective than the BAM complex in the folding of some substrate proteins.
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