PMID:12427258
| Citation |
Mallik, I, Smith, MA and Flower, AM (2002) Recognition of secretory proteins in Escherichia coli requires signals in addition to the signal sequence and slow folding. BMC Microbiol. 2:32 |
|---|---|
| Abstract |
The Sec-dependent protein export apparatus of Escherichia coli is very efficient at correctly identifying proteins to be exported from the cytoplasm. Even bacterial strains that carry prl mutations, which allow export of signal sequence-defective precursors, accurately differentiate between cytoplasmic and mutant secretory proteins. It was proposed previously that the basis for this precise discrimination is the slow folding rate of secretory proteins, resulting in binding by the secretory chaperone, SecB, and subsequent targeting to translocase. Based on this proposal, we hypothesized that a cytoplasmic protein containing a mutation that slows its rate of folding would be recognized by SecB and therefore targeted to the Sec pathway. In a Prl suppressor strain the mutant protein would be exported to the periplasm due to loss of ability to reject non-secretory proteins from the pathway. |
| Links | |
| Keywords |
Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Bacterial Proteins/secretion; Binding Sites; DNA-Binding Proteins; Endopeptidases/metabolism; Escherichia coli/genetics; Escherichia coli/metabolism; Mutation; Precipitin Tests; Protein Folding; Protein Sorting Signals/genetics; Protein Structure, Tertiary; Repressor Proteins/genetics; Repressor Proteins/physiology; Signal Transduction/physiology; Viral Proteins; Viral Regulatory and Accessory Proteins |
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