Proteomic dissection of potential signal recognition particle dependence in protein secretion by Bacillus subtilis
Autor: | Wim J. Quax, Rob Meima, Jan Maarten van Dijl, Michael Hecker, Geeske Zanen, Marc Kolkman, Jan D. H. Jongbloed, Haike Antelmann |
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Přispěvatelé: | Faculty of Science and Engineering, Cardiovascular Centre (CVC), Translational Immunology Groningen (TRIGR), Biopharmaceuticals, Discovery, Design and Delivery (BDDD), Nanotechnology and Biophysics in Medicine (NANOBIOMED) |
Jazyk: | angličtina |
Rok vydání: | 2006 |
Předmět: |
Proteomics
Signal peptide EXPRESSION Proteome Bacillus subtilis Biology Peptide Mapping Biochemistry Mass Spectrometry FtsY Bacterial Proteins Bacillus subtilisl protein secretion Extracellular signal recognition particle Electrophoresis Gel Two-Dimensional Secretion SMALL CYTOPLASMIC RNA Molecular Biology TARGETING PATHWAY Signal recognition particle RECEPTOR TRIGGER FACTOR Biological Transport biology.organism_classification GENE Peptide Fragments HOMOLOG Secretory protein Membrane protein ESCHERICHIA-COLI Ffh MEMBRANE REGULATOR |
Zdroj: | Proteomics, 6(12), 3636-3648. Wiley |
ISSN: | 1615-9853 |
Popis: | The bacterial signal recognition particle (SRP)-dependent pathway is believed to be a major targeting route for membrane proteins, as well as for subsets of secretory proteins. The present studies were aimed at an assessment of the role of two key components of SRP, namely Ffh and FtsY, in protein secretion by the Gram-positive bacterium Bacillus subtilis. Our results show that both components are important for the extracellular accumulation of proteins containing known signal peptides. Remarkably, extracellular accumulation of individual proteins was affected to different extents by depletion of Ffh or FtsY, at least under the conditions tested. Moreover, the observed Ffh or FtsY dependence of certain secretory proteins did not seem to correlate with signal peptide length or hydrophobicity. Although it is presently difficult to distinguish between direct and indirect effects, these findings suggest that other, yet unidentified, determinants in secretory proteins are also important for their SRP dependence. High-level production of homologous and heterologous secretory proteins was shown to result in elevated cellular Ffh and FtsY levels. This phenomenon is, most likely, due to post-transcriptional regulation. In conclusion, the present proteomic dissection of SRP-dependent extracellular protein accumulation provides exciting leads to identify novel determinants for interactions between secretory proteins and SRP. |
Databáze: | OpenAIRE |
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