Literature DB >> 12522254

Role of a highly conserved bacterial protein in outer membrane protein assembly.

Romé Voulhoux1, Martine P Bos, Jeroen Geurtsen, Maarten Mols, Jan Tommassen.   

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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Year:  2003        PMID: 12522254     DOI: 10.1126/science.1078973

Source DB:  PubMed          Journal:  Science        ISSN: 0036-8075            Impact factor:   47.728


  285 in total

Review 1.  Molecular basis of bacterial outer membrane permeability revisited.

Authors:  Hiroshi Nikaido
Journal:  Microbiol Mol Biol Rev       Date:  2003-12       Impact factor: 11.056

2.  Tob38, a novel essential component in the biogenesis of beta-barrel proteins of mitochondria.

Authors:  Thomas Waizenegger; Shukry J Habib; Maciej Lech; Dejana Mokranjac; Stefan A Paschen; Kai Hell; Walter Neupert; Doron Rapaport
Journal:  EMBO Rep       Date:  2004-06-18       Impact factor: 8.807

3.  Import pathways of chloroplast interior proteins and the outer-membrane protein OEP14 converge at Toc75.

Authors:  Shih-Long Tu; Lih-Jen Chen; Matthew D Smith; Yi-Shin Su; Danny J Schnell; Hsou-Min Li
Journal:  Plant Cell       Date:  2004-07-16       Impact factor: 11.277

4.  A hydrocarbon ruler measures palmitate in the enzymatic acylation of endotoxin.

Authors:  Victoria E Ahn; Eileen I Lo; Christian K Engel; Lu Chen; Peter M Hwang; Lewis E Kay; Russell E Bishop; Gilbert G Privé
Journal:  EMBO J       Date:  2004-07-22       Impact factor: 11.598

5.  Structure of the translocator domain of a bacterial autotransporter.

Authors:  Clasien J Oomen; Peter van Ulsen; Patrick van Gelder; Maya Feijen; Jan Tommassen; Piet Gros
Journal:  EMBO J       Date:  2004-03-11       Impact factor: 11.598

6.  Substitutions in the BamA β-barrel domain overcome the conditional lethal phenotype of a ΔbamB ΔbamE strain of Escherichia coli.

Authors:  Rene Tellez; Rajeev Misra
Journal:  J Bacteriol       Date:  2011-10-28       Impact factor: 3.490

7.  The prodomain of the Bordetella two-partner secretion pathway protein FhaB remains intracellular yet affects the conformation of the mature C-terminal domain.

Authors:  Christopher R Noël; Joseph Mazar; Jeffrey A Melvin; Jessica A Sexton; Peggy A Cotter
Journal:  Mol Microbiol       Date:  2012-10-05       Impact factor: 3.501

8.  Identification of novel surface proteins of Anaplasma phagocytophilum by affinity purification and proteomics.

Authors:  Yan Ge; Yasuko Rikihisa
Journal:  J Bacteriol       Date:  2007-08-31       Impact factor: 3.490

Review 9.  Contact-Dependent Growth Inhibition (CDI) and CdiB/CdiA Two-Partner Secretion Proteins.

Authors:  Julia L E Willett; Zachary C Ruhe; Celia W Goulding; David A Low; Christopher S Hayes
Journal:  J Mol Biol       Date:  2015-09-24       Impact factor: 5.469

10.  Autotransporter structure reveals intra-barrel cleavage followed by conformational changes.

Authors:  Travis J Barnard; Nathalie Dautin; Petra Lukacik; Harris D Bernstein; Susan K Buchanan
Journal:  Nat Struct Mol Biol       Date:  2007-11-11       Impact factor: 15.369

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