Abstract
The efficiency of secretion of Escherichia coli alkaline phosphatase depends on the presence in cells of a cytoplasmic chaperone - protein SecB. Secretion increases in the presence of this chaperone at 30°C, which is the most favorable for the interaction of SecB with the export-initiation domain found previously in the N-terminal region of the mature enzyme. This interaction most likely occurs in the region of the export domain, which is located close to the signal peptide and in complex with a translocational ATPase - protein SecA.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 985-990 |
| Number of pages | 6 |
| Journal | Biokhimiya |
| Volume | 66 |
| Issue number | 7 |
| State | Published - 2001 |
| Externally published | Yes |
Keywords
- Alkaline phosphatase
- Amino acid substitutions
- Chaperone SecB
- Escherichia coli
- Export domain
- Protein SecA
- Protein translocation
ASJC Scopus subject areas
- General Chemistry
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