ArticleThe Journal of biological chemistry2014
Evolutionary conservation in biogenesis of β-barrel proteins allows mitochondria to assemble a functional bacterial trimeric autotransporter protein.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 32 citations in OpenAlex.
- Identification of the adhesive domain of AtaA fromFrontiers in bioengineering and biotechnology · 2022Article
- Building Better Barrels - β-barrel Biogenesis and Insertion in Bacteria and Mitochondria.Journal of molecular biology · 2021Review
- Folding Control in the Path of Type 5 Secretion.Toxins · 2021Review
- BamA forms a translocation channel for polypeptide export across the bacterial outer membrane.Molecular cell · 2021Article
- The Biogenesis Process of VDAC - From Early Cytosolic Events to Its Final Membrane Integration.Frontiers in physiology · 2021Review
- Targeting and Insertion of Membrane Proteins in Mitochondria.Frontiers in cell and developmental biology · 2021Review
- Autotransporter-Mediated Display of Complement Receptor Ligands by Gram-Negative Bacteria Increases Antibody Responses and Limits Disease Severity.Pathogens (Basel, Switzerland) · 2020Article
- Mitochondrial-bacterial hybrids of BamA/Tob55 suggest variable requirements for the membrane integration of β-barrel proteins.Scientific reports · 2016Article
- Characterization of the targeting signal in mitochondrial β-barrel proteins.Nature communications · 2016Article
- Bipartite Topology of Treponema pallidum Repeat Proteins C/D and I: OUTER MEMBRANE INSERTION, TRIMERIZATION, AND PORIN FUNCTION REQUIRE A C-TERMINAL β-BARREL DOMAIN.The Journal of biological chemistry · 2015Article
- Inhibition of the β-barrel assembly machine by a peptide that binds BamD.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Yersinia adhesin A (YadA) belongs to a class of bacterial adhesins that form trimeric structures. Their mature form contains a passenger domain and a C-terminal β-domain that anchors the protein in the outer membrane (OM). Little is known about how precursors of such proteins cross the periplasm and assemble into the OM. In the present study we took advantage of the evolutionary conservation in the biogenesis of β-barrel proteins between bacteria and mitochondria. We previously observed that upon expression in yeast cells, bacterial β-barrel proteins including the transmembrane domain of YadA assemble into the mitochondrial OM. In the current study we found that when expressed in yeast cells both the monomeric and trimeric forms of full-length YadA were detected in mitochondria but only the trimeric species was fully integrated into the OM. The oligomeric form was exposed on the surface of the organelle in its native conformation and maintained its capacity to adhere to host cells. The co-expression of YadA with a mitochondria-targeted form of the bacterial periplasmic chaperone Skp, but not with SurA or SecB, resulted in enhanced levels of both forms of YadA. Taken together, these results indicate that the proper assembly of trimeric autotransporter can occur also in a system lacking the lipoproteins of the BAM machinery and is specifically enhanced by the chaperone Skp.
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