ArticleMolecular microbiology2019
Chaperone OsmY facilitates the biogenesis of a major family of autotransporters.
Article in Molecular microbiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- The translocation assembly module (TAM) catalyzes the assembly of bacterial outer membrane proteins in vitro.Nature communications · 2024Article
- Compensatory evolution of chromosomes and plasmids counteracts the plasmid fitness cost.Ecology and evolution · 2024Article
- The translocation assembly module (TAM) catalyzes the assembly of bacterial outer membrane proteinsbioRxiv : the preprint server for biology · 2024Article
- The Balance between Protealysin and Its Substrate, the Outer Membrane Protein OmpX, RegulatesInternational journal of molecular sciences · 2024Review
- Serratia marcescens DUF1471-Containing Protein SrfN Is Needed for Adaptation to Acid and Oxidative Stresses.mSphere · 2022Article
- Transcriptomic Analysis Revealed Antimicrobial Mechanisms ofInternational journal of molecular sciences · 2022Article
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- BonA frommBio · 2021Article
- Folding Control in the Path of Type 5 Secretion.Toxins · 2021Review
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- A metabolite binding protein moonlights as a bile-responsive chaperone.The EMBO journal · 2020Article
- Bam complex-mediated assembly of bacterial outer membrane proteins synthesized in an in vitro translation system.Scientific reports · 2020Article
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Authors and funding
5 authors.
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Abstract
OsmY is a widely conserved but poorly understood 20 kDa periplasmic protein. Using a folding biosensor, we previously obtained evidence that OsmY has molecular chaperone activity. To discover natural OsmY substrates, we screened for proteins that are destabilized and thus present at lower steady-state levels in an osmY-null strain. The abundance of an outer membrane protein called antigen 43 was substantially decreased and its β-barrel domain was undetectable in the outer membrane of an osmY-null strain. Antigen 43 is a member of the diffuse adherence family of autotransporters. Like strains that are defective in antigen 43 production, osmY-null mutants failed to undergo cellular autoaggregation. In vitro, OsmY assisted in the refolding of the antigen 43 β-barrel domain and protected it from added protease. Finally, an osmY-null strain that expressed two members of the diffuse adherence family of autotransporters that are distantly related to antigen 43, EhaA and TibA, contained reduced levels of the proteins and failed to undergo cellular autoaggregation. Taken together, our results indicate that OsmY is involved in the biogenesis of a major subset of autotransporters, a group of proteins that play key roles in bacterial pathogenesis.
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