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Role of a Highly Conserved Bacterial Protein in Outer Membrane Protein Assembly

Voulhoux, Romé, Bos, Martine P., Geurtsen, Jeroen, Mols, Maarten, Tommassen, Jan·2003·Science

Abstract

After transport across the cytoplasmic membrane, bacterial outer membrane proteins are assembled into the outer membrane. Meningococcal Omp85 is a highly conserved protein in Gram-negative bacteria, and its homolog Toc75 is a component of the chloroplast protein-import machinery. Omp85 appeared to be essential for viability, and unassembled forms of various outer membrane proteins accumulated upon Omp85 depletion. Immunofluorescence microscopy revealed decreased surface exposure of outer membrane proteins, which was particularly apparent at the cell-division planes. Thus, Omp85 is likely to play a role in outer membrane protein assembly.

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Metadata

Authors
Voulhoux, R., Bos, M. P., Geurtsen, J., Mols, M., & Tommassen, J.
Venue
Science
Published
2003-01-10
Volume
299
Issue
5604
Pages
262-265
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2085019401
Cited by
742
References
0
FWCI
20.60
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Role of a Highly Conserved Bacterial Protein in Outer Membrane Protein Assembly. https://app.cochat.ai/papers/10.1126/science.1078973
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Voulhoux, R., Bos, M. P., Geurtsen, J., Mols, M., & Tommassen, J. (2003). Role of a Highly Conserved Bacterial Protein in Outer Membrane Protein Assembly. Science. https://doi.org/10.1126/science.1078973

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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.