The DOI matches its Crossref record; 50 of the 50 references it cites were found in a registry or an index.
SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins.
Open accessAbstract
Little is known about either the process of periplasmic protein folding or how information concerning the folding state in this compartment is communicated. We present evidence that SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, is involved in the maturation and assembly of LamB. LamB is a trimeric outer membrane porin for maltodextrins as well as the bacteriophage lambda receptor in Escherichia coli. We demonstrate that SurA is involved in the conversion of unfolded monomers into a newly identified intermediate in LamB assembly, which behaves as a folded monomer. The absence of SurA blocks the assembly pathway and leads to accumulation of species prior to the folded monomer. These species also accumulate when the stress sigma factor sigmaE is induced by LamB overexpression. We suggest that accumulation of species prior to the generation of folded monomer is a stress signal sensed by sigmaE.
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Self-citationHeat shock proteins: molecular chaperones of protein biogenesis
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Release of outer membrane vesicles by Gram‐negative bacteria is a novel envelope stress response
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Metadata
- Authors
- Rouvière, P. E., & Gross, C. A.
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 1996-12-15
- Volume
- 10
- Issue
- 24
- Pages
- 3170-3182
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- OpenAlex
- W2044784863
- Cited by
- 324
- References
- 50
- Type
- posted content
- Language
- en
- Open access
- diamond
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- CoChat. (2026). Citation check: SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins. https://app.cochat.ai/papers/10.1101/gad.10.24.3170
- The paper
- Rouvière, P. E., & Gross, C. A. (1996). SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins. Genes & Development. https://doi.org/10.1101/gad.10.24.3170
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
