An alternative protein targeting pathway in Escherichia coli: studies on the role of FtsY

In Escherichia coli, a signal recognition particle (SRP) has been identified which binds specifically to the signal sequence of presecretory proteins and which appears to be essential for efficient translocation of a subset of proteins. In this study we have investigated the function of E. coli FtsY...

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Bibliographic Details
Published in:The EMBO journal 1994-05, Vol.13 (10), p.2289-2296
Main Authors: Luirink, J., Hagen‐Jongman, C.M., Weijden, C.C., Oudega, B., High, S., Dobberstein, B., Kusters, R.
Format: Article
Language:English
Subjects:
Bacterial Outer Membrane Proteins - metabolism
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Bacterial Proteins - physiology
Bacteriology
beta-Lactamases - metabolism
Biological and medical sciences
Biological Transport
Carrier Proteins - metabolism
Cell Compartmentation
Cloning, Molecular
Escherichia coli
Escherichia coli - genetics
Escherichia coli - growth & development
Escherichia coli - metabolism
Escherichia coli - ultrastructure
Escherichia coli Proteins
Fundamental and applied biological sciences. Psychology
Membrane Proteins - genetics
Membrane Proteins - metabolism
Microbiology
Periplasmic Binding Proteins
Permeability, membrane transport, intracellular transport
Protein Precursors - metabolism
Receptors, Cytoplasmic and Nuclear - genetics
Receptors, Cytoplasmic and Nuclear - metabolism
Receptors, Cytoplasmic and Nuclear - physiology
Receptors, Peptide - genetics
Receptors, Peptide - metabolism
Recombinant Proteins - metabolism
Signal Recognition Particle
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Summary:In Escherichia coli, a signal recognition particle (SRP) has been identified which binds specifically to the signal sequence of presecretory proteins and which appears to be essential for efficient translocation of a subset of proteins. In this study we have investigated the function of E. coli FtsY which shares sequence similarity with the alpha‐subunit of the eukaryotic SRP receptor (‘docking protein’) in the membrane of the endoplasmic reticulum. A strain was constructed which allows the conditional expression of FtsY. Depletion of FtsY is shown to cause the accumulation of the precursor form of beta‐lactamase, OmpF and ribose binding protein in vivo, whereas the processing of various other presecretory proteins is unaffected. Furthermore, FtsY‐depleted inverted cytoplasmic membrane vesicles are shown to be defective in the translocation of pre‐beta‐lactamase using an in vitro import assay. Subcellular localization studies revealed that FtsY is located in part at the cytoplasmic membrane with which it seems peripherally associated. These observations suggest that FtsY is the functional E. coli homolog of the mammalian SRP receptor.
ISSN:0261-4189
1460-2075
DOI:10.1002/j.1460-2075.1994.tb06511.x