ArticleJournal of molecular biology2019
The Role of SurA PPIase Domains in Preventing Aggregation of the Outer-Membrane Proteins tOmpA and OmpT.
Article in Journal of molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 34 citations in OpenAlex.
- Integration of Membrane Proteins into the Outer Membrane of Diderm Bacteria by the BAM Complex.Chemical reviews · 2026Review
- Article
- A human gut bacterium antagonizes neighboring bacteria by altering their protein-folding ability.Cell host & microbe · 2025Article
- Dual client binding sites in the ATP-independent chaperone SurA.Nature communications · 2024Article
- Outer membrane protein assembly mediated by BAM-SurA complexes.Nature communications · 2024Article
- The intrinsic macrolide resistome ofAntimicrobial agents and chemotherapy · 2024Article
- The chaperone PrsA2 regulates the secretion, stability, and folding of listeriolysin O duringmBio · 2024Article
- Roles of Nucleic Acids in Protein Folding, Aggregation, and Disease.ACS chemical biology · 2024Review
- High-throughput screening of BAM inhibitors in native membrane environment.Nature communications · 2023Article
- FkpA enhances membrane protein folding using an extensive interaction surface.Protein science : a publication of the Protein Society · 2023Article
- Interaction of the periplasmic chaperone SurA with the inner membrane protein secretion (SEC) machinery.The Biochemical journal · 2023Article
- SurA-like and Skp-like Proteins as Important Virulence Determinants of the Gram Negative Bacterial Pathogens.International journal of molecular sciences · 2022Review
- Dynamic interplay between the periplasmic chaperone SurA and the BAM complex in outer membrane protein folding.Communications biology · 2022Article
- Chaperones Skp and SurA dynamically expand unfolded OmpX and synergistically disassemble oligomeric aggregates.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The role of membrane destabilisation and protein dynamics in BAM catalysed OMP folding.Nature communications · 2021Article
- Molecular Basis of Essentiality of Early Critical Steps in the Lipopolysaccharide Biogenesis inInternational journal of molecular sciences · 2021Article
- Strategies for Rapid Identification ofFrontiers in cellular and infection microbiology · 2021Article
- SurA is a cryptically grooved chaperone that expands unfolded outer membrane proteins.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients.Nature communications · 2020Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
SurA is a conserved ATP-independent periplasmic chaperone involved in the biogenesis of outer-membrane proteins (OMPs). Escherichia coli SurA has a core domain and two peptidylprolyl isomerase (PPIase) domains, the role(s) of which remain unresolved. Here we show that while SurA homologues in early proteobacteria typically contain one or no PPIase domains, the presence of two PPIase domains is common in SurA in later proteobacteria, implying an evolutionary advantage for this domain architecture. Bioinformatics analysis of >350,000 OMP sequences showed that their length, hydrophobicity and aggregation propensity are similar across the proteobacterial classes, ruling out a simple correlation between SurA domain architecture and these properties of OMP sequences. To investigate the role of the PPIase domains in SurA activity, we deleted one or both PPIase domains from E.coli SurA and investigated the ability of the resulting proteins to bind and prevent the aggregation of tOmpA (19 kDa) and OmpT (33 kDa). The results show that wild-type SurA inhibits the aggregation of both OMPs, as do the cytoplasmic OMP chaperones trigger factor and SecB. However, while the ability of SurA to bind and prevent tOmpA aggregation does not depend on its PPIase domains, deletion of even a single PPIase domain ablates the ability of SurA to prevent OmpT aggregation. The results demonstrate that the core domain of SurA endows its generic chaperone ability, while the presence of PPIase domains enhances its chaperone activity for specific OMPs, suggesting one reason for the conservation of multiple PPIase domains in SurA in proteobacteria.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.