PMID:14597695

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Citation

Eser, M and Ehrmann, M (2003) SecA-dependent quality control of intracellular protein localization. Proc. Natl. Acad. Sci. U.S.A. 100:13231-4

Abstract

Complex secretion machineries mediate protein translocation across cellular membranes. These machines typically recognize their substrates via signal sequences, which are required for proper targeting to the translocon. We report that during posttranslational secretion the widely conserved targeting factor SecA performs a quality-control function that is based on a general chaperone activity. This quality-control mechanism involves assisted folding of signal sequenceless proteins, thereby excluding them from the secretion process. These results suggest that SecA channels proteins into one of two key pathways, posttranslational secretion or folding in the cytoplasm. Implications of this finding for intracellular protein localization are discussed.

Links

PubMed PMC263763 Online version:10.1073/pnas.2234410100

Keywords

Adenosine Triphosphatases/metabolism; Adenosine Triphosphatases/physiology; Alkaline Phosphatase; Amylases/chemistry; Bacterial Proteins; Citrate (si)-Synthase/chemistry; Cyclin-Dependent Kinases/chemistry; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Escherichia coli Proteins/physiology; Hydrogen-Ion Concentration; Membrane Transport Proteins/metabolism; Membrane Transport Proteins/physiology; Protein Folding; Protein Transport; Temperature; Time Factors

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